Enzyme Nomenclature

Continued from EC 2.7.4 to EC 2.7.6

EC 2.7.7

EC 2.7.7 Nucleotidyltransferases

Contents

See separate file for EC 2.7.7.51 to EC 2.7.7.103.

EC 2.7.7.1 nicotinamide-nucleotide adenylyltransferase
EC 2.7.7.2 FAD synthetase
EC 2.7.7.3 pantetheine-phosphate adenylyltransferase
EC 2.7.7.4 sulfate adenylyltransferase
EC 2.7.7.5 sulfate adenylyltransferase (ADP)
EC 2.7.7.6 DNA-directed RNA polymerase
EC 2.7.7.7 DNA-directed DNA polymerase
EC 2.7.7.8 polyribonucleotide nucleotidyltransferase
EC 2.7.7.9 UTP—glucose-1-phosphate uridylyltransferase
EC 2.7.7.10 UTP—hexose-1-phosphate uridylyltransferase
EC 2.7.7.11 UTP—xylose-1-phosphate uridylyltransferase
EC 2.7.7.12 UDP-glucose—hexose-1-phosphate uridylyltransferase
EC 2.7.7.13 mannose-1-phosphate guanylyltransferase
EC 2.7.7.14 ethanolamine-phosphate cytidylyltransferase
EC 2.7.7.15 choline-phosphate cytidylyltransferase
EC 2.7.7.16 now EC 3.1.27.5
EC 2.7.7.17 now EC 3.1.27.1
EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase
EC 2.7.7.19 polynucleotide adenylyltransferase
EC 2.7.7.20 deleted
EC 2.7.7.21 transferred now covered by EC 2.7.7.72
EC 2.7.7.22 mannose-1-phosphate guanylyltransferase (GDP)
EC 2.7.7.23 UDP-N-acetylglucosamine diphosphorylase
EC 2.7.7.24 glucose-1-phosphate thymidylyltransferase
EC 2.7.7.25 transferred now covered by EC 2.7.7.72
EC 2.7.7.26 now EC 3.1.27.3
EC 2.7.7.27 glucose-1-phosphate adenylyltransferase
EC 2.7.7.28 nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase
EC 2.7.7.29 identical to EC 2.7.7.28
EC 2.7.7.30 fucose-1-phosphate guanylyltransferase
EC 2.7.7.31 DNA nucleotidylexotransferase
EC 2.7.7.32 galactose-1-phosphate thymidylyltransferase
EC 2.7.7.33 glucose-1-phosphate cytidylyltransferase
EC 2.7.7.34 glucose-1-phosphate guanylyltransferase
EC 2.7.7.35 ADP ribose phosphorylase
EC 2.7.7.36 aldose-1-phosphate adenylyltransferase
EC 2.7.7.37 aldose-1-phosphate nucleotidyltransferase
EC 2.7.7.38 3-deoxy-manno-octulosonate cytidylyltransferase
EC 2.7.7.39 glycerol-3-phosphate cytidylyltransferase
EC 2.7.7.40 D-ribitol-5-phosphate cytidylyltransferase
EC 2.7.7.41 phosphatidate cytidylyltransferase
EC 2.7.7.42 [glutamine synthetase] adenylyltransferase
EC 2.7.7.43 N-acylneuraminate cytidylyltransferase
EC 2.7.7.44 glucuronate-1-phosphate uridylyltransferase
EC 2.7.7.45 guanosine-triphosphate guanylyltransferase
EC 2.7.7.46 gentamicin 2"-nucleotidyltransferase
EC 2.7.7.47 streptomycin 3"-adenylyltransferase
EC 2.7.7.48 RNA-directed RNA polymerase
EC 2.7.7.49 RNA-directed DNA polymerase
EC 2.7.7.50 mRNA guanylyltransferase
Continued with EC 2.7.7.51 to EC 2.7.7.103.


Entries

EC 2.7.7.1

Accepted name: nicotinamide-nucleotide adenylyltransferase

Reaction: ATP + nicotinamide ribonucleotide = diphosphate + NAD+

For diagram of reaction click here.

Other name(s): NAD+ pyrophosphorylase; adenosine triphosphate-nicotinamide mononucleotide transadenylase; ATP:NMN adenylyltransferase; diphosphopyridine nucleotide pyrophosphorylase; nicotinamide adenine dinucleotide pyrophosphorylase; nicotinamide mononucleotide adenylyltransferase; NMN adenylyltransferase

Systematic name: ATP:nicotinamide-nucleotide adenylyltransferase

Comments: Nicotinate nucleotide can also act as acceptor. See also EC 2.7.7.18 nicotinate-nucleotide adenylyltransferase.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9032-70-6

References:

1. Atkinson, M.R., Jackson, J.F. and Morton, R.K. Nicotinamide mononucleotide adenylyltransferase of pig-liver nuclei. The effects of nicotinamide mononucleotide concentration and pH on dinucleotide synthesis. Biochem. J. 80 (1961) 318-323.

2. Dahmen, W., Webb, B. and Preiss, J. The deamido-diphosphopyridine nucleotide and diphosphopyridine nucleotide pyrophosphorylases of Escherichia coli and yeast. Arch. Biochem. Biophys. 120 (1967) 440-450. [PMID: 4291828]

3. Kornberg, A. and Pricer, W.E. Enzymatic cleavage of diphosphopyridine nucleotide with radioactive pyrophosphate. J. Biol. Chem. 191 (1951) 535-541.

[EC 2.7.7.1 created 1961]

EC 2.7.7.2

Accepted name: FAD synthetase

Reaction: ATP + FMN = diphosphate + FAD

For diagram of reaction click here.

Other name(s): FAD pyrophosphorylase; riboflavin mononucleotide adenylyltransferase; adenosine triphosphate-riboflavin mononucleotide transadenylase; adenosine triphosphate-riboflavine mononucleotide transadenylase; riboflavin adenine dinucleotide pyrophosphorylase; riboflavine adenine dinucleotide adenylyltransferase; flavin adenine dinucleotide synthetase; FADS; FMN adenylyltransferase

Systematic name: ATP:FMN adenylyltransferase

Comments: Requires Mg2+ and is highly specific for ATP as phosphate donor [5]. The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates [3]. While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26, riboflavin kinase [3,5].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-37-3

References:

1. Giri, K.V., Rao, N.A., Cama, H.R. and Kumar, S.A. Studies on flavinadenine dinucleotide-synthesizing enzyme in plants. Biochem. J. 75 (1960) 381-386. [PMID: 13828163]

2. Schrecker, A.W. and Kornberg, A. Reversible enzymatic synthesis of flavin-adenine dinucleotide. J. Biol. Chem. 182 (1950) 795-803.

3. Sandoval, F.J. and Roje, S. An FMN hydrolase is fused to a riboflavin kinase homolog in plants. J. Biol. Chem. 280 (2005) 38337-38345. [PMID: 16183635]

4. Oka, M. and McCormick, D.B. Complete purification and general characterization of FAD synthetase from rat liver. J. Biol. Chem. 262 (1987) 7418-7422. [PMID: 3034893]

5. Brizio, C., Galluccio, M., Wait, R., Torchetti, E.M., Bafunno, V., Accardi, R., Gianazza, E., Indiveri, C. and Barile, M. Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase. Biochem. Biophys. Res. Commun. 344 (2006) 1008-1016. [PMID: 16643857]

[EC 2.7.7.2 created 1961, modified 2007]

EC 2.7.7.3

Accepted name: pantetheine-phosphate adenylyltransferase

Reaction: ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA

For diagram of reaction click here.

Other name(s): dephospho-CoA pyrophosphorylase; pantetheine phosphate adenylyltransferase; dephospho-coenzyme A pyrophosphorylase; 3'-dephospho-CoA pyrophosphorylase

Systematic name: ATP:pantetheine-4'-phosphate adenylyltransferase

Comments: The enzyme from several bacteria (e.g. Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-99-7

References:

1. Hoagland, M.B. and Novelli, G.D. Biosynthesis of coenzyme A from phosphopantetheine and of pantetheine from pantothenate. J. Biol. Chem. 207 (1954) 767-773.

2. Novelli, G.D. Enzymatic synthesis and structure of CoA. Fed. Proc. 12 (1953) 675-682.

3. Martin, D.P. and Drueckhammer, D.G. Separate enzymes catalyze the final two steps of coenzyme A biosynthesis in Brevibacterium ammoniagenes: purification of pantetheine phosphate adenylyltransferase. Biochem. Biophys. Res. Commun. 192 (1993) 1155-1161. [PMID: 8389542]

4. Geerlof, A., Lewendon, A. and Shaw, W.V. Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli. J. Biol. Chem. 274 (1999) 27105-27111. [PMID: 10480925]

5. Izard, T., Geerlof, A., Lewendon, A. and Barker, J.J. Cubic crystals of phosphopantetheine adenylyltransferase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 55 1999) 1226-1228. [PMID: 10329792]

[EC 2.7.7.3 created 1961, modified 2002]

EC 2.7.7.4

Accepted name: sulfate adenylyltransferase

Reaction: ATP + sulfate = diphosphate + adenylyl sulfate

Glossary: 3'-phosphoadenylyl sulfate = PAPS

Other name(s): ATP-sulfurylase; adenosine-5'-triphosphate sulfurylase; adenosinetriphosphate sulfurylase; adenylylsulfate pyrophosphorylase; ATP sulfurylase; ATP-sulfurylase; sulfurylase

Systematic name: ATP:sulfate adenylyltransferase

Comments: The human phosphoadenosine-phosphosulfate synthase (PAPSS) system is a bifunctional enzyme (fusion product of two catalytic activities). In a first step, sulfate adenylyltransferase catalyses the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate. The second step is catalysed by the adenylylsulfate kinase portion of 3'-phosphoadenosine 5'-phosphosulfate synthase, which involves the formation of PAPS from enzyme-bound APS and ATP. In contrast, in bacteria, yeast, fungi and plants, the formation of PAPS is carried out by two individual polypeptides, sulfate adenylyltransferase (EC 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25).

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9012-39-9

References:

1. Bandurski, R.S., Wilson, L.G. and Squires, C.L. The mechanism of "active sulfate" formation. J. Am. Chem. Soc. 78 (1956) 6408-6409.

2. Hilz, H. and Lipmann, F. The enzymatic activation of sulfate. Proc. Natl. Acad. Sci. USA 41 (1955) 880-890.

3. Venkatachalam, K.V., Akita, H., Strott, C. Molecular cloning, expression and characterization of human bifunctional 3'-phosphoadenosine-5'-phosphosulfate synthase and its functional domains. J. Biol. Chem. 273 (1998) 19311-19320. [PMID: 9668121]

[EC 2.7.7.4 created 1961, modified 1999]

EC 2.7.7.5

Accepted name: sulfate adenylyltransferase (ADP)

Reaction: ADP + sulfate = phosphate + adenylyl sulfate

Other name(s): ADP-sulfurylase; sulfate (adenosine diphosphate) adenylyltransferase; adenosine diphosphate sulfurylase

Systematic name: ADP:sulfate adenylyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9027-70-7

References:

1. Grunberg-Manago, M., del Campillo-Campbell, A., Dondon, L. and Michelson, A.M. Yeast ADP-sulfurylase catalyzing an exchange between orthophosphate and the terminal phosphate of nucleoside diphosphates. Biochim. Biophys. Acta 123 (1966) 1-16. [PMID: 5964041]

2. Robbins, P.W. and Lipmann, F. Isolation and identification of active sulfate. J. Biol. Chem. 229 (1957) 837-851.

[EC 2.7.7.5 created 1961]

EC 2.7.7.6

Accepted name: DNA-directed RNA polymerase

Reaction: nucleoside triphosphate + RNAn = diphosphate + RNAn+1

Other name(s): RNA polymerase; RNA nucleotidyltransferase (DNA-directed); RNA polymerase I; RNA polymerase II; RNA polymerase III; RNA nucleotidyltransferase (DNA-directed); C RNA formation factors; deoxyribonucleic acid-dependent ribonucleic acid polymerase; DNA-dependent ribonucleate nucleotidyltransferase; DNA-dependent RNA nucleotidyltransferase; DNA-dependent RNA polymerase; ribonucleate nucleotidyltransferase; ribonucleate polymerase; C ribonucleic acid formation factors;ribonucleic acid nucleotidyltransferase; ribonucleic acid polymerase; ribonucleic acid transcriptase; ribonucleic polymerase; ribonucleic transcriptase; C RNA formation factors; RNA nucleotidyltransferase; RNA transcriptase; transcriptase; RNA nucleotidyltransferase I

Systematic name: nucleoside-triphosphate:RNA nucleotidyltransferase (DNA-directed)

Comments: Catalyses DNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. In eukaryotes, three forms of the enzyme have been distinguished on the basis of sensitivity to α-amanitin, and the type of RNA synthesized. See also EC 2.7.7.19 (polynucleotide adenylyltransferase) and EC 2.7.7.48 (RNA-directed RNA polymerase).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9014-24-8

References:

1. Krakow, J.S. and Ochoa, S. RNA polymerase from Azotobacter vinelandii. Methods Enzymol. 6 (1963) 11-17.

2. Mans, R.J. and Walter, T.J. Transfer RNA-primed oligoadenylate synthesis in maize seedlings. II. Primer, substrate and metal specificities and size of product. Biochim. Biophys. Acta 247 (1971) 113-121. [PMID: 4946277]

3. Roeder, R.G. in Losick, R. and Chamberlin, M. (Eds.), RNA Polymerase, Cold Spring Harbor Laboratory, 1976, p. 285.

4. Sheldon, R., Jurale, C.and Kates, J. Detection of polyadenylic acid sequences in viral and eukaryotic RNA(poly(U)-cellulose columns-poly(U) filters-fiberglass-HeLa cells-bacteriophage T4). Proc. Natl. Acad. Sci. USA 69 (1972) 417-421. [PMID: 4501121]

5. Weaver, R.F., Blatti, S.P. and Rutter, W.J. Molecular structures of DNA-dependent RNA polymerases (II) from calf thymus and rat liver. Proc. Natl. Acad. Sci. USA 68 (1971) 2994-2999. [PMID: 5289245]

[EC 2.7.7.6 created 1961, modified 1981, modified 1982, modified 1989]

EC 2.7.7.7

Accepted name: DNA-directed DNA polymerase

Reaction: a 2′-deoxyribonucleoside 5′-triphosphate + DNAn = diphosphate + DNAn+1

Other name(s): DNA polymerase I; DNA polymerase II; DNA polymerase III; DNA polymerase α; DNA polymerase β; DNA polymerase γ; DNA nucleotidyltransferase (DNA-directed); deoxyribonucleate nucleotidyltransferase; deoxynucleate polymerase; deoxyribonucleic acid duplicase; deoxyribonucleic acid polymerase; deoxyribonucleic duplicase; deoxyribonucleic polymerase; deoxyribonucleic polymerase I; DNA duplicase; DNA nucleotidyltransferase; DNA polymerase; DNA replicase; DNA-dependent DNA polymerase; duplicase; Klenow fragment; sequenase; Taq DNA polymerase; Taq Pol I; Tca DNA polymerase

Systematic name: 2′-deoxyribonucleoside-5′-triphosphate:DNA deoxynucleotidyltransferase (DNA-directed)

Comments: Catalyses DNA-template-directed extension of the 3'- end of a DNA strand by one nucleotide at a time. Cannot initiate a chain de novo. Requires a primer, which may be DNA or RNA. See also EC 2.7.7.49 RNA-directed DNA polymerase.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9012-90-2

References:

1. Bollum, F.J. Calf thymus polymerase. J. Biol. Chem. 235 (1960) 2399-2403.

2. Falaschi, A. and Kornberg, A. Biochemical studies of bacterial sporulation. II. Deoxy-ribonucleic acid polymerase in spores of Bacillus subtilis. J. Biol. Chem. 241 (1966) 1478-1482. [PMID: 4957767]

3. Lehman, I.R., Bessman, M.J., Simms, E.S. and Kornberg, A. Enzymatic synthesis of deoxyribonucleic acid. I. Preparation of substrates and partial purification of an enzyme from Escherichia coli. J. Biol. Chem. 233 (1958) 163-170.

4. Richardson, C.C., Schildkraut, C.L., Aposhian, H.V. and Kornberg, A. Enzymatic synthesis of deoxyribonucleic acid. XIV. Further purification and properties of deoxyribonucleic acid polymerase of Escherichia coli. J. Biol. Chem. 239 (1964) 222-232.

5. Schachman, H.K., Adler, J., Radding, C.M., Lehman, I.R. and Kornberg, A. Enzymatic synthesis of deoxyribonucleic acid. VII. Synthesis of a polymer of deoxyadenylate and deoxythymidylate. J. Biol. Chem. 235 (1960) 3242-3249.

6. Zimmerman, B.K. Purification and properties of deoxyribonucleic acid polymerase from Micrococcus lysodeikticus. J. Biol. Chem. 241 (1966) 2035-2041. [PMID: 5946628]

[EC 2.7.7.7 created 1961, modified 1981, modified 1982]

EC 2.7.7.8

Accepted name: polyribonucleotide nucleotidyltransferase

Reaction: RNAn+1 + phosphate = RNAn + a nucleoside diphosphate

Other name(s): polynucleotide phosphorylase; PNPase; nucleoside diphosphate:polynucleotidyl transferase; polyribonucleotide nucleotidyltransferase; polynucleotide phosphorylase; polyribonucleotide phosphorylase

Systematic name: polyribonucleotide:phosphate nucleotidyltransferase

Comments: ADP, IDP, GDP, UDP and CDP can act as donors.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9014-12-4

References:

1. Hakim, A.A. Synthetic activity of polynucleotide phosphorylase from sperm. Nature 183 (1959) 334 only.

2. Littauer, U.Z. and Kornberg, A. Reversible synthesis of polyribonucleotides with an enzyme from Escherichia coli. J. Biol. Chem. 226 (1957) 1077-1092.

3. Ochoa, S. and Mii, S. Enzymatic synthesis of polynucleotides. IV. Purification and properties of polynucleotide phosphorylase from Azotobacter vinelandii. J. Biol. Chem. 236 (1961) 3303-3311.

[EC 2.7.7.8 created 1961]

EC 2.7.7.9

Accepted name: UTP—glucose-1-phosphate uridylyltransferase

Reaction: UTP + α-D-glucose 1-phosphate = diphosphate + UDP-glucose

For diagram of reaction click here.

Other name(s): UDP glucose pyrophosphorylase; glucose-1-phosphate uridylyltransferase; UDPG phosphorylase; UDPG pyrophosphorylase; uridine 5'-diphosphoglucose pyrophosphorylase; uridine diphosphoglucose pyrophosphorylase; uridine diphosphate-D-glucose pyrophosphorylase; uridine-diphosphate glucose pyrophosphorylase

Systematic name: UTP:α-D-glucose-1-phosphate uridylyltransferase

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-22-6

References:

1. Kalckar, H.M. The role of phosphoglycosyl compounds in the biosynthesis of nucleosides and nucleotides. Biochim. Biophys. Acta 12 (1953) 250-264.

2. Kamogawa, A. and Kurahashi, K. Purification and properties of uridinediphosphate glucose pyrophosphorylase from Escherichia coli K12. J. Biochem. (Tokyo) 57 (1965) 758-765. [PMID: 4284510]

3. Lobelle-Rich, P.A. and Reeves, R.E. Separation and characterization of two UTP-utilizing hexose phosphate uridylyltransferases from Entamoeba histolytica. Mol. Biochem. Parasitol. 7 (1983) 173-182. [PMID: 6304512]

4. Smith, E.E.B. and Mills, G.T. The uridyl transferase of mammary gland. Biochim. Biophys. Acta 18 (1955) 152 only.

5. Turnquist, R.L., Gillett, T.A. and Hansen, R.G. Uridine diphosphate glucose pyrophosphorylase. Crystallization and properties of the enzyme from rabbit liver and species comparisons. J. Biol. Chem. 249 (1974) 7695-7700. [PMID: 4436332]

[EC 2.7.7.9 created 1961]

EC 2.7.7.10

Accepted name: UTP—hexose-1-phosphate uridylyltransferase

Reaction: UTP + α-D-galactose 1-phosphate = diphosphate + UDP-α-D-galactose

For diagram of reaction click here.

Other name(s): galactose-1-phosphate uridylyltransferase; galactose 1-phosphate uridylyltransferase; α-D-galactose 1-phosphate uridylyltransferase; galactose 1-phosphate uridyltransferase; UDPgalactose pyrophosphorylase; uridine diphosphate galactose pyrophosphorylase; uridine diphosphogalactose pyrophosphorylase

Systematic name: UTP:α-D-hexose-1-phosphate uridylyltransferase

Comments: α-D-Glucose 1-phosphate can also act as acceptor, but more slowly.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9016-11-9

References:

1. Isselbacher, K.J. A mammalian uridinediphosphate galactose pyrophosphorylase. J. Biol. Chem. 232 (1958) 429-444.

2. Kalckar, H.M. The role of phosphoglycosyl compounds in the biosynthesis of nucleosides and nucleotides. Biochim. Biophys. Acta 12 (1953) 250-264.

3. Lee, L., Kimura, A. and Tochikura, T. Purification and properties of UDP-glucose (UDP-galactose) pyrophosphorylase from Bifidobacterium bifidum. J. Biochem. (Tokyo) 86 (1979) 923-928. [PMID: 500588]

4. Lobelle-Rich, P.A. and Reeves, R.E. Separation and characterization of two UTP-utilizing hexose phosphate uridylyltransferases from Entamoeba histolytica. Mol. Biochem. Parasitol. 7 (1983) 173-182. [PMID: 6304512]

[EC 2.7.7.10 created 1961]

EC 2.7.7.11

Accepted name: UTP—xylose-1-phosphate uridylyltransferase

Reaction: UTP + α-D-xylose 1-phosphate = diphosphate + UDP-xylose

For diagram of reaction click here.

Other name(s): xylose-1-phosphate uridylyltransferase; uridylyltransferase, xylose 1-phosphate; UDP-xylose pyrophosphorylase; uridine diphosphoxylose pyrophosphorylase; xylose 1-phosphate uridylyltransferase

Systematic name: UTP:α-D-xylose-1-phosphate uridylyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9026-20-4

References:

1. Ginsburg, V., Neufeld, E.F. and Hassid, W.Z. Enzymatic synthesis of uridine diphosphate xylose and uridine diphosphate arabinose. Proc. Natl. Acad. Sci. USA 42 (1956) 333-335.

[EC 2.7.7.11 created 1961]

EC 2.7.7.12

Accepted name: UDP-glucose—hexose-1-phosphate uridylyltransferase

Reaction: UDP-α-D-glucose + α-D-galactose 1-phosphate = α-D-glucose 1-phosphate + UDP-α-D-galactose

For diagram of reaction click here.

Other name(s): uridyl transferase; hexose-1-phosphate uridylyltransferase; uridyltransferase; hexose 1-phosphate uridyltransferase

Systematic name: UDP-α-D-glucose:α-D-galactose-1-phosphate uridylyltransferase

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-21-5

References:

1. Kalckar, H.M., Braganca, B. and Munch-Petersen, A. Uridyl transferases and the formation of uridinediphosphogalactose. Nature 172 (1953) 1038 only. [PMID: 13111247]

2. Kurahashi, K. and Sugimura, A. Purification and properties of galactose 1-phosphate uridyl transferase from Escherichia coli. J. Biol. Chem. 235 (1960) 940-946. [PMID: 14412847]

3. Mayes, J.S. and Hansen, R.G. Galactose 1-phosphate uridyl transferase. Methods Enzymol. 9 (1966) 708-713.

4. Saito, S., Ozutsumi, M. and Kurahashi, K. Galactose 1-phosphate uridylyltransferase of Escherichia coli. II. Further purification and characterization. J. Biol. Chem. 242 (1967) 2362-2368. [PMID: 5338129]

5. Smith, E.E.B. and Mills, G.T. Uridyl transferase of mammary gland. Biochim. Biophys. Acta 18 (1955) 152 only. [PMID: 13260264]

[EC 2.7.7.12 created 1961]

EC 2.7.7.13

Accepted name: mannose-1-phosphate guanylyltransferase

Reaction: GTP + α-D-mannose 1-phosphate = diphosphate + GDP-mannose

For diagram click here.

Other name(s): GTP—mannose-1-phosphate guanylyltransferase; PIM-GMP (phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase); GDP-mannose pyrophosphorylase; guanosine 5'-diphospho-D-mannose pyrophosphorylase; guanosine diphosphomannose pyrophosphorylase; guanosine triphosphate-mannose 1-phosphate guanylyltransferase; mannose 1-phosphate guanylyltransferase (guanosine triphosphate)

Systematic name: GTP:α-D-mannose-1-phosphate guanylyltransferase

Comments: The bacterial enzyme can also use ITP and dGTP as donors.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 37278-24-3

References:

1. Munch-Peterson, A. Enzymatic synthesis and phosphorolysis of guanosine diphosphate mannose. Arch. Biochem. Biophys. 55 (1955) 592-593.

2. Preiss, J. and Wood, E. Sugar nucleotide reactions in Arthrobacter. I. Guanosinediphosphate mannose pyrophosphorylase: purification and properties. J. Biol. Chem. 239 (1964) 3119-3126.

[EC 2.7.7.13 created 1961, modified 1976]

EC 2.7.7.14

Accepted name: ethanolamine-phosphate cytidylyltransferase

Reaction: CTP + ethanolamine phosphate = diphosphate + CDP-ethanolamine

Other name(s): phosphorylethanolamine transferase; ET; CTP-phosphoethanolamine cytidylyltransferase; phosphoethanolamine cytidylyltransferase; ethanolamine phosphate cytidylyltransferase

Systematic name: CTP:ethanolamine-phosphate cytidylyltransferase

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-33-9

References:

1. Kennedy, E.P. and Weiss, S.B. The function of cytidine coenzymes in the biosynthesis of phospholipides. J. Biol. Chem. 222 (1956) 193-214.

2. Sundler, R. Ethanolaminephosphate cytidylyltransferase. Purification and characterization of the enzyme from rat liver. J. Biol. Chem. 250 (1975) 8585-8590. [PMID: 241749]

3. Visedo-Gonzalez, E. and Dixon, H.B.F. 2-Aminoethylarsonic acid as an analogue of ethanolamine phosphate. Endowment of ethanolamine-phosphate cytidylyltransferase with CTP pyrophosphatase activity. Biochem. J. 260 (1989) 299-301. [PMID: 2549956]

[EC 2.7.7.14 created 1961]

EC 2.7.7.15

Accepted name: choline-phosphate cytidylyltransferase

Reaction: CTP + phosphocholine = diphosphate + CDP-choline

Other name(s): phosphorylcholine transferase; CDP-choline pyrophosphorylase; CDP-choline synthetase; choline phosphate cytidylyltransferase; CTP-phosphocholine cytidylyltransferase; CTP:phosphorylcholine cytidylyltransferase; cytidine diphosphocholine pyrophosphorylase; phosphocholine cytidylyltransferase; phosphorylcholine cytidylyltransferase; phosphorylcholine:CTP cytidylyltransferase; CTP:choline-phosphate cytidylyltransferase

Systematic name: CTP:phosphocholine cytidylyltransferase

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-34-0

References:

1. Borkenhagen, L.F. and Kennedy, E.P. The enzymatic synthesis of cytidine diphosphate choline. J. Biol. Chem. 227 (1957) 951-962.

2. Kennedy, E.P. and Weiss, S.B. The function of cytidine coenzymes in the biosynthesis of phospholipides. J. Biol. Chem. 222 (1956) 193-214.

3. Williams-Ashman, H.G. and Banks, J. Participation of cytidine coenzymes in the metabolism of choline by seminal vesicles. J. Biol. Chem. 223 (1956) 509-521.

[EC 2.7.7.15 created 1961]

[EC 2.7.7.16 Transferred entry: now EC 3.1.27.5 pancreatic ribonuclease (EC 2.7.7.16 created 1961, deleted 1972, [transferred to EC 3.1.4.22, deleted 1980])]

[EC 2.7.7.17 Transferred entry: now EC 3.1.27.1 ribonuclease T2 (EC 2.7.7.17 created 1965, deleted 1972, [transferred to EC 3.1.4.23, deleted 1980])]

EC 2.7.7.18

Accepted name: nicotinate-nucleotide adenylyltransferase

Reaction: ATP + nicotinate β-D-ribonucleotide = diphosphate + deamido-NAD+

For diagram of reaction click here.

Other name(s): deamido-NAD+ pyrophosphorylase; nicotinate mononucleotide adenylyltransferase; deamidonicotinamide adenine dinucleotide pyrophosphorylase; NaMN-ATase; nicotinic acid mononucleotide adenylyltransferase; ATP:nicotinate-ribonucleotide adenylyltransferase

Systematic name: ATP:nicotinate-β-D-ribonucleotide adenylyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-98-6

References:

1. Imsande, J. Pathway of diphosphopyridine nucleotide biosynthesis in Escherichia coli. J. Biol. Chem. 236 (1961) 1494-1497.

[EC 2.7.7.18 created 1965]

EC 2.7.7.19

Accepted name: polynucleotide adenylyltransferase

Reaction: ATP + RNAn = diphosphate + RNAn+1

Other name(s): NTP polymerase; RNA adenylating enzyme; AMP polynucleotidylexotransferase; ATP-polynucleotide adenylyltransferase; ATP:polynucleotidylexotransferase; poly(A) polymerase; poly(A) synthetase; polyadenylate nucleotidyltransferase; polyadenylate polymerase; polyadenylate synthetase; polyadenylic acid polymerase; polyadenylic polymerase; terminal riboadenylate transferase; poly(A) hydrolase; RNA formation factors, PF1; adenosine triphosphate:ribonucleic acid adenylyltransferase

Systematic name: ATP:polynucleotide adenylyltransferase

Comments: Also acts slowly with CTP. Catalyses template-independent extension of the 3'- end of a DNA strand by one nucleotide at a time. Cannot initiate a chain de novo. The primer, depending on the source of the enzyme, may be an RNA or DNA fragment, or oligo(A) bearing a 3'-OH terminal group. See also EC 2.7.7.6 DNA-directed RNA polymerase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-30-6

References:

1. August, J.T., Ortiz, P.J. and Hurwitz, J. Ribonucleic acid-dependent ribonucleotide incorporation. I. Purification and properties of the enzyme. J. Biol. Chem. 237 (1962) 3786-3793.

2. Edmonds, M. and Abrams, R. Polynucleotide biosynthesis: formation of a sequence of adenylate units from adenosine triphosphate by an enzyme from thymus nuclei. J. Biol. Chem. 235 (1960) 1142-1149.

3. Gottesman, M.E. and Canellakis, E.S. The terminal nucleotidyltransferases of calf thymus nuclei. J. Biol. Chem. 241 (1966) 4339-4352. [PMID: 4288534]

4. Krakow, J.S., Coutsogeorgopoulos, C. and Canellakis, E.S. Studies on the incorporation of deoxyribonucleic acid. Biochim. Biophys. Acta 55 (1962) 639-650.

5. Mans, R.J. and Walter, T.J. Transfer RNA-primed oligoadenylate synthesis in maize seedlings. II. Primer, substrate and metal specificities and size of product. Biochim. Biophys. Acta 247 (1971) 113-121. [PMID: 4946277]

6. Sheldon, R., Jurale, C. and Kates, J. Detection of polyadenylic acid sequences in viral and eukaryotic RNA(polu(U)-cellulose columns-poly(U) filters-fiberglass-HeLa cells-bacteriophage T4). Proc. Natl. Acad. Sci. USA 69 (1972) 417-421. [PMID: 4501121]

[EC 2.7.7.19 created 1965]

[EC 2.7.7.20 Deleted entry: This entry was identical with EC 2.7.7.25 tRNA adenylyltransferase (EC 2.7.7.20 created 1965, deleted 1972)]

[EC 2.7.7.21 Transferred entry: tRNA cytidylyltransferase. Now EC 2.7.7.72, CCA tRNA nucleotidyltransferase (EC 2.7.7.21 created 1965, deleted 2010)]

EC 2.7.7.22

Accepted name: mannose-1-phosphate guanylyltransferase (GDP)

Reaction: GDP + α-D-mannose 1-phosphate = phosphate + GDP-mannose

For diagram click here.

Other name(s): GDP mannose phosphorylase; mannose 1-phosphate (guanosine diphosphate) guanylyltransferase; GDP mannose phosphorylase; GDP-mannose 1-phosphate guanylyltransferase; guanosine diphosphate-mannose 1-phosphate guanylyltransferase; guanosine diphosphomannose phosphorylase; mannose 1-phosphate guanylyltransferase; GDP:D-mannose-1-phosphate guanylyltransferase

Systematic name: GDP:α-D-mannose-1-phosphate guanylyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9026-31-7

References:

1. Carminatti, H. and Cabib, E. Phosphorolysis of the pyrophosphate bond of some nucleotides. Biochim. Biophys. Acta 53 (1961) 417-419.

[EC 2.7.7.22 created 1965, modified 1976]

EC 2.7.7.23

Accepted name: UDP-N-acetylglucosamine diphosphorylase

Reaction: UTP + N-acetyl-α-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-α-D-glucosamine

For diagram of reaction click here

Other name(s): UDP-N-acetylglucosamine pyrophosphorylase; uridine diphosphoacetylglucosamine pyrophosphorylase; UTP:2-acetamido-2-deoxy-α-D-glucose-1-phosphate uridylyltransferase; UDP-GlcNAc pyrophosphorylase; GlmU uridylyltransferase; Acetylglucosamine 1-phosphate uridylyltransferase; UDP-acetylglucosamine pyrophosphorylase; uridine diphosphate-N-acetylglucosamine pyrophosphorylase; uridine diphosphoacetylglucosamine phosphorylase; acetylglucosamine 1-phosphate uridylyltransferase

Systematic name: UTP:N-acetyl-α-D-glucosamine-1-phosphate uridylyltransferase

Comments: Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Hemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase [3,4,6]. The enzyme from plants and animals is also active toward N-acetyl-α-D-galactosamine 1-phosphate (cf. EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase) [5,7], while the bacterial enzyme shows low activity toward that substrate [4].

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9023-06-7

References:

1. Pattabiramin, T.N. and Bachhawat, B.K. Purification of uridine diphosphoacetylglucosamine pyrophosphorylase from sheep brain. Biochim. Biophys. Acta 50 (1961) 129-134. [PMID: 13733356]

2. Strominger, J.L. and Smith, M.S. Uridine diphosphoacetylglucosamine pyrophosphorylase. J. Biol. Chem. 234 (1959) 1822-1827. [PMID: 13672971]

3. Mengin-Lecreulx, D. and van Heijenoort, J. Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis. J. Bacteriol. 176 (1994) 5788-5795. [PMID: 8083170]

4. Gehring, A.M., Lees, W.J., Mindiola, D.J., Walsh, C.T. and Brown, E.D. Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli. Biochemistry 35 (1996) 579-585. [PMID: 8555230]

5. Wang-Gillam, A., Pastuszak, I. and Elbein, A.D. A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc. J. Biol. Chem. 273 (1998) 27055-27057. [PMID: 9765219]

6. Olsen, L.R. and Roderick, S.L. Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites. Biochemistry 40 (2001) 1913-1921. [PMID: 11329257]

7. Peneff, C., Ferrari, P., Charrier, V., Taburet, Y., Monnier, C., Zamboni, V., Winter, J., Harnois, M., Fassy, F. and Bourne, Y. Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture. EMBO J. 20 (2001) 6191-6202. [PMID: 11707391]

[EC 2.7.7.23 created 1965, modified 2012]

EC 2.7.7.24

Accepted name: glucose-1-phosphate thymidylyltransferase

Reaction: dTTP + α-D-glucose 1-phosphate = diphosphate + dTDP-α-Dglucose

For diagram click here.

Other names: glucose 1-phosphate thymidylyltransferase; dTDP-glucose synthase; dTDP-glucose pyrophosphorylase; thymidine diphosphoglucose pyrophosphorylase; thymidine diphosphate glucose pyrophosphorylase; TDP-glucose pyrophosphorylase

Systematic name: dTTP:α-D-glucose-1-phosphate thymidylyltransferase

Comments: Involved in the biosynthesis of L-rhamnose in bacteria.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9026-03-3

References:

1. Kornfeld, S. and Glaser, L. The enzymic synthesis of thymidine-linked sugars. I. Thymidine diphosphate glucose. J. Biol. Chem. 236 (1961) 1791-1794.

2. Pazur, J.H. and Shuey, E.W. The enzymatic synthesis of thymidine diphosphate glucose and its conversion to thymidine diphosphate rhamnose. J. Biol. Chem. 236 (1961) 1780-1785.

[EC 2.7.7.24 created 1965]

[EC 2.7.7.25 Transferred entry: tRNA adenylyltransferase. Now EC 2.7.7.72, CCA tRNA nucleotidyltransferase (EC 2.7.7.25 created 1965, deleted 2010)]

[EC 2.7.7.26 Transferred entry: now EC 3.1.27.3 ribonuclease T1 (EC 2.7.7.26 created 1961 as EC 3.1.4.8, transferred 1965 to EC 2.7.7.26, deleted 1972)]

EC 2.7.7.27

Accepted name: glucose-1-phosphate adenylyltransferase

Reaction: ATP + α-D-glucose 1-phosphate = diphosphate + ADP-glucose

Other name(s): ADP glucose pyrophosphorylase; glucose 1-phosphate adenylyltransferase; adenosine diphosphate glucose pyrophosphorylase; adenosine diphosphoglucose pyrophosphorylase; ADP-glucose pyrophosphorylase; ADP-glucose synthase; ADP-glucose synthetase; ADPG pyrophosphorylase; ADP:α-D-glucose-1-phosphate adenylyltransferase

Systematic name: ATP:α-D-glucose-1-phosphate adenylyltransferase

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9027-71-8

References:

1. Ghosh, H.P. and Preiss, J. Adenosine diphosphate glucose pyrophosphorylase. A regulatory enzyme in the biosynthesis of starch in spinach leaf chloroplasts. J. Biol. Chem. 241 (1966) 4491-4504. [PMID: 5922972]

2. Shen, L. and Preiss, J. Biosynthesis of bacterial glycogen. I. Purification and properties of the adenosine diphosphoglucose pyrophosphorylase of Arthrobacter species NRRL B1973. J. Biol. Chem. 240 (1965) 2334-2340.

[EC 2.7.7.27 created 1972]

EC 2.7.7.28

Accepted name: nucleoside-triphosphate-aldose-1-phosphate nucleotidyltransferase

Reaction: nucleoside triphosphate + α-D-aldose 1-phosphate = diphosphate + NDP-hexose

Other name(s): NDP hexose pyrophosphorylase; hexose 1-phosphate nucleotidyltransferase; hexose nucleotidylating enzyme; nucleoside diphosphohexose pyrophosphorylase; hexose-1-phosphate guanylyltransferase; GTP:α-D-hexose-1-phosphate guanylyltransferase; GDP hexose pyrophosphorylase; guanosine diphosphohexose pyrophosphorylase; nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase; NTP:hexose-1-phosphate nucleotidyltransferase

Systematic name: NTP:α-D-aldose-1-phosphate nucleotidyltransferase

Comments: In decreasing order of activity, guanosine, inosine and adenosine diphosphate hexoses are substrates in the reverse reaction, with either glucose or mannose as the sugar.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-26-5

References:

1. Verachtert, H., Rodriguez, P., Bass, S.T. and Hansen, R.G. Purification and properties of guanosine diphosphate hexose pyrophosphorylase from mammalian tissues. J. Biol. Chem. 241 (1966) 2007-2013. [PMID: 5946626]

2. Hansen, R.G., Verachtert, H., Rodriguez, P. and Bass, S.T. GDP-hexose pyrophosphorylase from liver. Methods Enzymol. 8 (1966) 269-271.

[EC 2.7.7.28 created 1972, modified 2004 (EC 2.7.7.29 created 1972, incorporated 2004)]

[EC 2.7.7.29 Deleted entry: hexose-1-phosphate guanylyltransferase. Enzyme is not specific for GTP and therefore is identical to EC 2.7.7.28, nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase (EC 2.7.7.29 created 1972, deleted 2004)]

EC 2.7.7.30

Accepted name: fucose-1-phosphate guanylyltransferase

Reaction: GTP + β-L-fucose 1-phosphate = diphosphate + GDP-L-fucose

For diagram click here.

Other name(s): GDP fucose pyrophosphorylase; guanosine diphosphate L-fucose pyrophosphorylase; GDP-L-fucose pyrophosphorylase; GDP-fucose pyrophosphorylase; GTP:L-fucose-1-phosphate guanylyltransferase

Systematic name: GTP:β-L-fucose-1-phosphate guanylyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9033-14-1

References:

1. Ishihara, H. and Heath, E.C. The metabolism of L-fucose. IV. The biosynthesis of guanosine diphosphate L-fucose in porcine liver. J. Biol. Chem. 243 (1968) 1110-1115. [PMID: 5646162]

[EC 2.7.7.30 created 1972]

EC 2.7.7.31

Accepted name: DNA nucleotidylexotransferase

Reaction: 2'-deoxyribonucleoside 5'-triphosphate + DNAn = diphosphate + DNAn+1

Other name(s): terminal deoxyribonucleotidyltransferase; terminal addition enzyme; addase; deoxynucleotidyl terminal transferase; deoxyribonucleic acid nucleotidyltransferase; deoxyribonucleic nucleotidyltransferase; terminal deoxynucleotide transferase; TdT

Systematic name: 2'-deoxyribonucleoside-5'-triphosphate:DNA deoxynucleotidylexotransferase

Comments: Catalyses template-independent extension of the 3'- end of a DNA strand by one nucleotide at a time. Cannot initiate a chain de novo. The nucleoside may be ribo- or 2'-deoxyribo-.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-67-2

References:

1. Bollum, F.J. Deoxynucleotide-polymerizing enzymes of calf thymus gland. V. Homogeneous terminal deoxynucleotidyl transferase. J. Biol. Chem. 246 (1971) 909-916. [PMID: 5543689]

2. Gottesman, M.E. and Canellakis, E.S. The terminal nucleotidyltransferases of calf thymus nuclei. J. Biol. Chem. 241 (1966) 4339-4352. [PMID: 4288534]

3. Krakow, J.S., Coutsogeorgopoulos, C. and Canellakis, E.S. Studies on the incorporation of deoxyribonucleic acid. Biochim. Biophys. Acta 55 (1962) 639-650.

[EC 2.7.7.31 created 1972]

EC 2.7.7.32

Accepted name: galactose-1-phosphate thymidylyltransferase

Reaction: dTTP + α-D-galactose 1-phosphate = diphosphate + dTDP-galactose

Other name(s): dTDP galactose pyrophosphorylase; galactose 1-phosphate thymidylyl transferase; thymidine diphosphogalactose pyrophosphorylase; thymidine triphosphate:α-D-galactose 1-phosphate thymidylyltransferase

Systematic name: dTTP:α-D-galactose-1-phosphate thymidylyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9023-25-0

References:

1. Pazur, J.H. and Anderson, J.S. Thymidine triphosphate: α-D-galactose 1-phosphate thymidylyltransferase from Streptococcus faecalis grown on D-galactose. J. Biol. Chem. 238 (1963) 3155-3160.

[EC 2.7.7.32 created 1972]

EC 2.7.7.33

Accepted name: glucose-1-phosphate cytidylyltransferase

Reaction: CTP + α-D-glucose 1-phosphate = diphosphate + CDP-glucose

Other name(s): CDP glucose pyrophosphorylase; cytidine diphosphoglucose pyrophosphorylase; cytidine diphosphate glucose pyrophosphorylase; cytidine diphosphate-D-glucose pyrophosphorylase; CTP:D-glucose-1-phosphate cytidylyltransferase

Systematic name: CTP:α-D-glucose-1-phosphate cytidylyltransferase

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9027-10-5

References:

1. Mayer, R.M. and Ginsburg, V. Purification and properties of cytidine diphosphate D-glucose pyrophosphorylase from Salmonella paratyphi A. J. Biol. Chem. 240 (1965) 1900-1904.

[EC 2.7.7.33 created 1972]

EC 2.7.7.34

Accepted name: glucose-1-phosphate guanylyltransferase

Reaction: GTP + α-D-glucose 1-phosphate = diphosphate + GDP-glucose

For diagram of reaction click here.

Other name(s): GDP glucose pyrophosphorylase; guanosine diphosphoglucose pyrophosphorylase

Systematic name: GTP:α-D-glucose-1-phosphate guanylyltransferase

Comments: Also acts, more slowly, on D-mannose 1-phosphate.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9033-13-0

References:

1. Danishefsky, I. and Heritier-Watkins, O. Nucleoside diphosphate glucose pyrophosphorylases in mast cell tumors. Biochim. Biophys. Acta 139 (1967) 349-357. [PMID: 6034677]

[EC 2.7.7.34 created 1972]

EC 2.7.7.35

Accepted name: ADP ribose phosphorylase

Reaction: ADP + D-ribose 5-phosphate = phosphate + ADP-D-ribose

Glossary: ADP-D-ribose = adenosine 5'-(5-deoxy-D-ribofuranos-5-yl diphosphate)

Other name(s): ; ribose-5-phosphate adenylyltransferase (ambiguous); adenosine diphosphoribose phosphorylase (ambiguous)

Systematic name: ADP:D-ribose-5-phosphate adenylyltransferase

Comments: The enzyme, characterized from the single-celled alga Euglena gracilis, catalyses an irreversible reaction in the direction of ADP formation. cf. EC 2.7.7.96, ADP-D-ribose pyrophosphorylase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9054-55-1

References:

1. Evans, W.R. and San Pietro, A. Phosphorolysis of adenosine diphosphoribose. Arch. Biochem. Biophys. 113 (1966) 236-244. [PMID: 4287446]

2. Stern, A.I. and Avron, M. An adenosine 5'-diphosphate ribose:orthophosphate adenylyltransferase from Euglena gracilis. Biochim. Biophys. Acta 118 (1966) 577-591. [PMID: 5970863]

[EC 2.7.7.35 created 1972, modified 2016]

EC 2.7.7.36

Accepted name: aldose-1-phosphate adenylyltransferase

Reaction: ADP + α-D-aldose 1-phosphate = phosphate + ADP-aldose

Other name(s): sugar-1-phosphate adenylyltransferase; ADPaldose phosphorylase; adenosine diphosphosugar phosphorylase; ADP sugar phosphorylase; adenosine diphosphate glucose:orthophosphate adenylyltransferase; ADP:aldose-1-phosphate adenylyltransferase

Systematic name: ADP:α-D-aldose-1-phosphate adenylyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37278-27-6

References:

1. Dankert, M., Gonçalves, I.R.J. and Recondo, E. Adenosine diphosphate glucose: orthophosphate adenylyltransferase in wheat germ. Biochim. Biophys. Acta 81 (1964) 78-85.

2. Passeron, S., Recondo, E. and Dankert, M. Biosynthesis of adenosine diphosphate D-hexoses. Biochim. Biophys. Acta 89 (1964) 372-374.

[EC 2.7.7.36 created 1972, modified 1986]

EC 2.7.7.37

Accepted name: aldose-1-phosphate nucleotidyltransferase

Reaction: NDP + α-D-aldose 1-phosphate = phosphate + NDP-aldose

For diagram of reaction click here.

Other name(s): sugar-1-phosphate nucleotidyltransferase; NDPaldose phosphorylase; glucose 1-phosphate inosityltransferase; NDP sugar phosphorylase; nucleoside diphosphosugar phosphorylase; sugar phosphate nucleotidyltransferase; nucleoside diphosphate sugar:orthophosphate nucleotidyltransferase; sugar nucleotide phosphorylase; NDP:aldose-1-phosphate nucleotidyltransferase

Systematic name: NDP:α-D-aldose-1-phosphate nucleotidyltransferase

Comments: The enzyme works on a variety of α-D-aldose 1-phosphates and β-L-aldose 1-phosphates (which have the same anomeric configuration as the former; see 2-Carb-6.2).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9033-61-8

References:

1. Cabib, E., Carminatti, H. and Woyskovsky, N.M. Phosphorolysis of the pyrophosphate bond of sugar nucleotides. II. Purification and properties of the enzyme. J. Biol. Chem. 240 (1965) 2114-2121. [PMID: 14299635]

[EC 2.7.7.37 created 1972, modified 1986]

EC 2.7.7.38

Accepted name: 3-deoxy-manno-octulosonate cytidylyltransferase

Reaction: CTP + 3-deoxy-D-manno-octulosonate = diphosphate + CMP-3-deoxy-D-manno-octulosonate

Other name(s): CMP-3-deoxy-D-manno-octulosonate pyrophosphorylase; 2-keto-3-deoxyoctonate cytidylyltransferase; 3-Deoxy-D-manno-octulosonate cytidylyltransferase; CMP-3-deoxy-D-manno-octulosonate synthetase; CMP-KDO synthetase; CTP:CMP-3-deoxy-D-manno-octulosonate cytidylyltransferase; cytidine monophospho-3-deoxy-D-manno-octulosonate pyrophosphorylase

Systematic name: CTP:3-deoxy-D-manno-octulosonate cytidylyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37278-28-7

References:

1. Ghalambor, M.A. and Heath, E.C. The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. IV. Purification and properties of cytidine monophosphate 3-deoxy-D-manno-octulosonate synthetase. J. Biol. Chem. 241 (1966) 3216-3221. [PMID: 5330266]

[EC 2.7.7.38 created 1972]

EC 2.7.7.39

Accepted name: glycerol-3-phosphate cytidylyltransferase

Reaction: CTP + sn-glycerol 3-phosphate = diphosphate + CDP-glycerol

Other name(s): CDP-glycerol pyrophosphorylase; cytidine diphosphoglycerol pyrophosphorylase; cytidine diphosphate glycerol pyrophosphorylase; CTP:glycerol 3-phosphate cytidylyltransferase; Gro-PCT; tagD (gene name); tarD (gene name)

Systematic name: CTP:sn-glycerol-3-phosphate cytidylyltransferase

Comments: Involved in the biosynthesis of teichoic acid linkage units in bacterial cell walls.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-11-6

References:

1. Shaw, D.R.D. Pyrophosphorolysis and enzymic synthesis of cytidine diphosphate glycerol and cytidine diphosphate ribitol. Biochem. J. 82 (1962) 297-312. [PMID: 13911452]

2. Park, Y.S., Sweitzer, T.D., Dixon, J.E. and Kent, C. Expression, purification, and characterization of CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis. J. Biol. Chem. 268 (1993) 16648-16654. [PMID: 8393871]

3. Sanker, S., Campbell, H.A. and Kent, C. Negative cooperativity of substrate binding but not enzyme activity in wild-type and mutant forms of CTP:glycerol-3-phosphate cytidylyltransferase. J. Biol. Chem. 276 (2001) 37922-37928. [PMID: 11487587]

4. Badurina, D.S., Zolli-Juran, M. and Brown, E.D. CTP:glycerol 3-phosphate cytidylyltransferase (TarD) from Staphylococcus aureus catalyzes the cytidylyl transfer via an ordered Bi-Bi reaction mechanism with micromolar K(m) values. Biochim. Biophys. Acta 1646 (2003) 196-206. [PMID: 12637027]

5. Pattridge, K.A., Weber, C.H., Friesen, J.A., Sanker, S., Kent, C. and Ludwig, M.L. Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis. J. Biol. Chem. 278 (2003) 51863-51871. [PMID: 14506262]

[EC 2.7.7.39 created 1972]

EC 2.7.7.40

Accepted name: D-ribitol-5-phosphate cytidylyltransferase

Reaction: CTP + D-ribitol 5-phosphate = diphosphate + CDP-ribitol

Other name(s): CDP ribitol pyrophosphorylase; cytidine diphosphate ribitol pyrophosphorylase; ribitol 5-phosphate cytidylyltransferase; cytidine diphosphoribitol pyrophosphorylase

Systematic name: CTP:D-ribitol-5-phosphate cytidylyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9027-07-0

References:

1. Shaw, D.R.D. Pyrophosphorolysis and enzymic synthesis of cytidine diphosphate glycerol and cytidine diphosphate ribitol. Biochem. J. 82 (1962) 297-312.

[EC 2.7.7.40 created 1972]

EC 2.7.7.41

Accepted name: phosphatidate cytidylyltransferase

Reaction: CTP + phosphatidate = diphosphate + CDP-diacylglycerol

Other name(s): CDP diglyceride pyrophosphorylase; CDP-diacylglycerol synthase; CDP-diacylglyceride synthetase; cytidine diphosphoglyceride pyrophosphorylase; phosphatidate cytidyltransferase; phosphatidic acid cytidylyltransferase; CTP:1,2-diacylglycerophosphate-cytidyl transferase; CTP-diacylglycerol synthetase; DAG synthetase; CDP-DG

Systematic name: CTP:phosphatidate cytidylyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9067-83-8

References:

1. Carter, J.R. and Kennedy, E.P. Enzymatic synthesis of cytidine diphosphate diglyceride. J. Lipid Res. 7 (1966) 678-683. [PMID: 4291255]

2. McCaman, R.E. and Finnerty, W.R. Biosynthesis of cytidine diphosphate-diglyceride by a particulate fraction from Micrococcus cerificans. J. Biol. Chem. 243 (1968) 5074-5080. [PMID: 5679981]

3. Petzold, G.L. and Agranoff, B.W. The biosynthesis of cytidine diphosphate diglyceride by embryonic chick brain. J. Biol. Chem. 242 (1967) 1187-1191. [PMID: 6067194]

[EC 2.7.7.41 created 1972]

EC 2.7.7.42

Accepted name: [glutamine synthetase] adenylyltransferase

Reaction: ATP + [glutamine synthetase]-L-tyrosine = diphosphate + [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine

Other name(s): glutamine-synthetase adenylyltransferase; ATP:glutamine synthetase adenylyltransferase; adenosine triphosphate:glutamine synthetase adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine adenylyltransferase; [glutamate—ammonia-ligase] adenylyltransferase

Systematic name: ATP:[glutamine synthetase]-L-tyrosine adenylyltransferase

Comments: This bacterial enzyme adenylates a tyrosine residue of EC 6.3.1.2, glutamine synthetase. The enzyme is bifunctional, and also catalyses a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC 2.7.7.89, [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase) [7,8]. The two activities are present on separate domains.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9077-66-1

References:

1. Ebner, E., Wolf, D., Gancedo, C., Elsasser, S. and Holzer, H. ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties. Eur. J. Biochem. 14 (1970) 535-544. [PMID: 4920894]

2. Kingdon, H.S., Shapiro, B.M. and Stadtman, E.R. Regulation of glutamine synthetase. 8. ATP: glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations in the regulatory properties of glutamine synthetase. Proc. Natl. Acad. Sci. USA 58 (1967) 1703-1710. [PMID: 4867671]

3. Mecke, D., Wulff, K. and Holzer, H. Characterization of a glutamine synthetase inactivating enzyme from Escherichia coli. Biochem. Biophys. Res. Commun. 24 (1966) 452-458. [PMID: 5338440]

4. Mecke, D., Wulff, K. and Holzer, H. Metabolit-induzierte Inaktivierung von Glutaminsynthetase aus Escherichia coli im zellfreien System. Biochim. Biophys. Acta 128 (1966) 559-567.

5. Shapiro, B.M. and Stadtman, E.R. 5'-Adenylyl-O-tyrosine. The novel phosphodiester residue of adenylylated glutamine synthetase from Escherichia coli. J. Biol. Chem. 243 (1968) 3769-3771. [PMID: 4298074]

6. Wolf, D., Ebner, E. and Hinze, H. Inactivation, stabilization and some properties of ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Eur. J. Biochem. 25 (1972) 239-244. [PMID: 4402680]

7. Jaggi, R., van Heeswijk, W.C., Westerhoff, H.V., Ollis, D.L. and Vasudevan, S.G. The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction. EMBO J. 16 (1997) 5562-5571. [PMID: 9312015]

8. Xu, Y., Zhang, R., Joachimiak, A., Carr, P.D., Huber, T., Vasudevan, S.G. and Ollis, D.L. Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase. Structure 12 (2004) 861-869. [PMID: 15130478]

[EC 2.7.7.42 created 1972, modified 2016]

EC 2.7.7.43

Accepted name: N-acylneuraminate cytidylyltransferase

Reaction: CTP + N-acylneuraminate = diphosphate + CMP-N-acylneuraminate

For diagram of reaction click here.

Other name(s): CMP-sialate pyrophosphorylase; CMP-sialate synthase; cytidine 5'-monophosphosialic acid synthetase; CMP-Neu5Ac synthetase; CMP-NeuAc synthetase; acylneuraminate cytidyltransferase; CMP-N-acetylneuraminate synthetase; CMP-N-acetylneuraminate synthase; CMP-N-acetylneuraminic acid synthase; CMP-NANA synthetase; CMP-sialate synthetase; CMP-sialic synthetase; cytidine 5'-monophospho-N-acetylneuraminic acid synthetase; cytidine 5-monophosphate N-acetylneuraminic acid synthetase; cytidine monophosphosialic acid synthetase; cytidine monophosphoacetylneuraminic synthetase; cytidine monophosphosialate pyrophosphorylase; cytidine monophosphosialate synthetase; acetylneuraminate cytidylyltransferase

Systematic name: CTP:N-acylneuraminate cytidylyltransferase

Comments: Acts on N-acetyl- and N-glycolyl- derivatives.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9067-82-7

References:

1. Kean, E.L. and Roseman, S. The sialic acids. X. Purification and properties of cytidine 5'-monophosphosialic acid synthetase. J. Biol. Chem. 241 (1966) 5643-5650. [PMID: 4288894]

[EC 2.7.7.43 created 1972]

EC 2.7.7.44

Accepted name: glucuronate-1-phosphate uridylyltransferase

Reaction: UTP + 1-phospho-α-D-glucuronate = diphosphate + UDP-glucuronate

For diagram of reaction click here.

Other names: UDP-glucuronate pyrophosphorylase; UDP-D-glucuronic acid pyrophosphorylase; UDP-glucuronic acid pyrophosphorylase; uridine diphosphoglucuronic pyrophosphorylase

Systematic name: UTP:1-phospho-α-D-glucuronate uridylyltransferase

Comments: Also acts slowly with CTP.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 52228-05-4

References:

1. Roberts, R.M. The formation of uridine diphosphate-glucuronic acid in plants. Uridine diphosphate-glucuronic acid pyrophosphorylase from barley seedlings. J. Biol. Chem. 246 (1971) 4995-5002. [PMID: 5570433]

[EC 2.7.7.44 created 1976]

EC 2.7.7.45

Accepted name: guanosine-triphosphate guanylyltransferase

Reaction: 2 GTP = diphosphate + P1,P4-bis(5'-guanosyl) tetraphosphate

Other names: diguanosine tetraphosphate synthetase; GTP-GTP guanylyltransferase; Gp4G synthetase; guanosine triphosphate-guanose triphosphate guanylyltransferase

Systematic name: GTP:GTP guanylyltransferase

Comments: Also acts, more slowly, on GDP to form P1,P3-bis(5'-guanosyl) triphosphate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 54576-89-5

References:

1. Warner, A.H., Beers, P.C. and Huang, F.L. Biosynthesis of the diguanosine nucleotides. I. Purification and properties of an enzyme from yolk platelets of brine shrimp embryos. Can. J. Biochem. 52 (1974) 231-240. [PMID: 4208243]

[EC 2.7.7.45 created 1976]

EC 2.7.7.46

Accepted name: gentamicin 2"-nucleotidyltransferase

Reaction: nucleoside triphosphate + gentamicin = diphosphate + 2"-nucleotidylgentamicin

Other names: gentamicin 2"-adenylyltransferase; aminoglycoside adenylyltransferase; gentamycin 2"-nucleotidyltransferase

Systematic name: NTP:gentamicin 2"-nucleotidyltransferase

Comments: ATP, dATP, CTP, ITP and GTP can act as donors; kanamycin, tobramycin and sisomicin can also act as acceptors. The nucleotidyl residue is transferred to the 2-hydroxy of the 3-amino-3-deoxy-D-glucose moiety in the antibiotic.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 62213-33-6

References:

1. Angelatou, F., Litsas, S.B. and Kontomichalou, P. Purification and properties of two gentamicin-modifying enzymes, coded by a single plasmid pPK237 originating from Pseudomonas aeruginosa. J. Antibiot. 35 (1982) 235-244. [PMID: 6281224]

2. Naganawa, H., Yagisawa, M., Kondo, S., Takeuchi, T. and Umezawa, H. The structure determination of an enzymatic inactivation product of 3',4'-dideoxykanamycin B. J. Antibiot. 24 (1971) 913-914. [PMID: 4946513]

3. Yagisawa, M., Naganawa, H., Kondo, S., Hamada, M., Takeuchi, T. and Umezawa, H. Adenylyldideoxykanamycin B, a product of the inactivation of dideoxykanamycin B by Escherichia coli carrying R factor. J. Antibiot. 24 (1971) 911-912. [PMID: 4946512]

[EC 2.7.7.46 created 1976]

EC 2.7.7.47

Accepted name: streptomycin 3"-adenylyltransferase

Reaction: ATP + streptomycin = diphosphate + 3"-adenylylstreptomycin

Other names: streptomycin adenylate synthetase; streptomycin adenyltransferase; streptomycin adenylylase; streptomycin adenylyltransferase; streptomycin-spectinomycin adenylyltransferase; AAD (3"); aminoglycoside 3"-adenylyltransferase

Systematic name: ATP:streptomycin 3"-adenylyltransferase

Comments: Also acts on spectinomycin.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 52660-23-8

References:

1. Hartwood, J.H. and Smith, D.H. Resistance factor-mediated streptomycin resistance. J. Bacteriol. 97 (1969) 1262-1271. [PMID: 4887506]

[EC 2.7.7.47 created 1976]

EC 2.7.7.48

Accepted name: RNA-directed RNA polymerase

Reaction: nucleoside triphosphate + RNAn = diphosphate + RNAn+1

Other name(s): RNA nucleotidyltransferase (RNA-directed); RNA nucleotidyltransferase (RNA-directed); RNA-dependent ribonucleate nucleotidyltransferase; 3D polymerase; PB1 proteins; PB2 proteins; phage f2 replicase; polymerase L; Q-β replicase; phage f2 replicase; ribonucleic acid replicase; ribonucleic acid-dependent ribonucleate nucleotidyltransferase; ribonucleic acid-dependent ribonucleic acid polymerase; ribonucleic replicase; ribonucleic synthetase; RNA replicase; RNA synthetase; RNA transcriptase; RNA-dependent ribonucleate nucleotidyltransferase; RDRP; RNA-dependent RNA polymerase; RNA-dependent RNA replicase; transcriptase

Systematic name: nucleoside-triphosphate:RNA nucleotidyltransferase (RNA-directed)

Comments: Catalyses RNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. See also EC 2.7.7.6 DNA-directed RNA polymerase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9026-28-2

References:

1. August, J.T., Cooper, S., Shapiro, L. and Zinder, N.D. RNA phage induced RNA polymerase. Cold Spring Harbour Symp. Quant. Biol. 28 (1963) 95-97.

2. Haruna, J., Nozu, K., Ohtaka, Y. and Spiegelman, S. An RNA "Replicase" induced by and selective for a viral RNA: isolation and properties. Proc. Natl. Acad. Sci. USA 50 (1963) 905-911. [PMID: 14082356]

3. Weismann, C., Simon, L. and Ochoa, S. Induction by an RNA phage of an enzyme catalyzing incorporation of ribonucleotides into ribonucleic acid. Proc. Natl. Acad. Sci. USA 49 (1963) 407-414. [PMID: 13999778]

[EC 2.7.7.48 created 1981, modified 1982]

EC 2.7.7.49

Accepted name: RNA-directed DNA polymerase

Reaction: a 2'-deoxyribonucleoside 5'-triphosphate + DNAn = diphosphate + DNAn+1

Other name(s): DNA nucleotidyltransferase (RNA-directed); reverse transcriptase; revertase; RNA-dependent deoxyribonucleate nucleotidyltransferase; RNA revertase; RNA-dependent DNA polymerase; RNA-instructed DNA polymerase; RT

Systematic name: 2'-deoxyribonucleoside-5'-triphosphate:DNA deoxynucleotidyltransferase (RNA-directed)

Comments: Catalyses RNA-template-directed extension of the 3'- end of a DNA strand by one deoxynucleotide at a time. Cannot initiate a chain de novo. Requires an RNA or DNA primer. DNA can also serve as template. See also EC 2.7.7.7 DNA-directed DNA polymerase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9068-38-6

References:

1. Baltimore, D. RNA-dependent DNA polymerase in virions of RNA tumour viruses. Nature 226 (1970) 1209-1211. [PMID: 4316300]

2. Temin, H. and Mizutani, S. RNA-dependent DNA polymerase in virions of Rous sarcoma virus. Nature 226 (1970) 1211-1213. [PMID: 4316301]

[EC 2.7.7.49 created 1981, modified 1982]

EC 2.7.7.50

Accepted name: mRNA guanylyltransferase

Reaction: GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA

Glossary: G(5')pppPur-mRNA = mRNA containing a guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue

Other name(s): mRNA capping enzyme; messenger RNA guanylyltransferase; Protein λ2

Systematic name: GTP:mRNA guanylyltransferase

Comments: The enzyme can also modify synthetic poly(A) and poly(G) to form the structures m7G(5')pppAn and m7G(5')pppGn.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 56941-23-2

References:

1. Ensinger, M.J., Martin, S.A., Paoletti, E. and Moss, B. Modification of the 5'-terminus of mRNA by soluble guanylyl and methyl transferases from vaccinia virus. Proc. Natl. Acad. Sci. USA 72 (1975) 2525-2529. [PMID: 1058472]

2. Groner, Y., Gilbao, E. and Aviv, H. Methylation and capping of RNA polymerase II primary transcripts by HeLa nuclear homogenates. Biochemistry 17 (1978) 977-982. [PMID: 629955]

3. Itoh, N., Yamada, H., Kaziro, Y. and Mizumoto, K. Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. Large scale purification, subunit functions, and subcellular localization. J. Biol. Chem. 262 (1987) 1989-1995. [PMID: 3029058]

4. Martin, S.A. and Moss, B. Modification of RNA by mRNA guanylyltransferase and mRNA (guanine-7-)methyltransferase from vaccinia virions. J. Biol. Chem. 250 (1975) 9330-9335. [PMID: 1194287]

5. Martin, S.A., Paoletti, E. and Moss, B. Purification of mRNA guanylyltransferase and mRNA (guanine-7-)methyltransferase from vaccinia virions. J. Biol. Chem. 250 (1975) 9322-9329. [PMID: 1194286]

[EC 2.7.7.50 created 1981]


Continued with EC 2.7.7.51 to EC 2.7.7.103
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