Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB)

Changes to the Enzyme List

The entries below are proposed additions and amendments to the Enzyme Nomenclature list. They were prepared for the NC-IUBMB by Keith Tipton, Sinéad Boyce and Hal Dixon and were put on the web by Gerry Moss. Comments and suggestions on enzyme classification and nomenclature may be sent to Professor K.F. Tipton (ktipton@tcd.ie) or Dr S. Boyce (sboyce@tcd.ie), Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland. These entries were made public February 2001 and approved April 2001.

An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.


[EC 1.1.1.242 Transferred entry: now EC 1.3.1.69 zeatin reductase (EC 1.1.1.242 created 1992, deleted 2001)]

EC 1.1.1.266

Recommended name: dTDP-4-dehydro-6-deoxyglucose reductase

Reaction: dTDP-D-fucose + NADP = dTDP-4-dehydro-6-deoxy-D-glucose + NADPH2

For reaction pathway click here.

Other name(s): dTDP-4-keto-6-deoxyglucose reductase

Systematic name: dTDP-D-fucose:NADP oxidoreductase

Comments: The enzyme from the gram-negative bacterium Actinobacillus actinomycetemcomitans forms activated fucose for incorporation into capsular polysaccharide.

Reference:

1. Yoshida, Y., Nakano, Y., Nezu, T., Yamashita, Y. and Koga, T. A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucose. J. Biol. Chem. 274 (1999) 16933-16939. [Medline UI: 99287888]

[EC 1.1.1.266 created 2001]

*EC 1.1.3.28

Recommended name: nucleoside oxidase

Reaction: inosine + O2 = 9-riburonosylhypoxanthine + H2O

Systematic name: nucleoside:oxygen 5'-oxidoreductase

Comments: Other purine and pyrimidine nucleosides (as well as 2'-deoxynucleosides) are substrates, but ribose and nucleotides are not substrates. The overall reaction takes place in two separate steps:

(1) 2 inosine + O2 = 2 5'-dehydroinosine + 2 H2O;
(2) 2 5'-dehydroinosine + O2 = 2 9-riburonosylhypoxanthine + 2 H2O

with the 5'-dehydro nucleoside being released from the enzyme to serve as substrate for the second reaction. This enzyme differs from EC 1.1.3.39, nucleoside oxidase (H2O2-forming), as it produces water rather than hydrogen peroxide.

References:

1. Isono, Y., Sudo, T. and Hoshino, M. Purification and reaction of a new enzyme, nucleoside oxidase. Agric. Biol. Chem. 53 (1989) 1663-1669.

2. Isono, Y., Sudo, T. and Hoshino, M. Properties of a new enzyme, nucleoside oxidase, from Pseudomonas maltophilia LB-86. Agric. Biol. Chem. 53 (1989) 1671-1677.

[EC 1.1.3.28 created 1992, modified 2001]

EC 1.1.3.39

Recommended name: nucleoside oxidase (H2O2-forming)

Reaction: adenosine + 2 O2 = 9-riburonosyladenine + 2 H2O2

Systematic name: nucleoside:oxygen 5'-oxidoreductase (H2O2-forming)

Comments: A heme-containing flavoprotein (FAD). Other purine and pyrimidine nucleosides (as well as 2'-deoxynucleosides and arabinosides) are substrates, but ribose and nucleotides are not substrates. The overall reaction takes place in two separate steps:

(1) adenosine + O2 = 5'-dehydroadenosine + H2O2
(2) 5'-dehydroadenosine + O2 = 9-riburonosyladenine + H2O2

with the 5'-dehydro nucleoside being released from the enzyme to serve as substrate for the second reaction. This enzyme differs from EC 1.1.3.28, nucleoside oxidase, as it produces hydrogen peroxide rather than water.

References:

1. Koga, S., Ogawa, J., Cheng, L.Y., Choi, Y.M., Yamada, H. and Shimizu, S. Nucleoside oxidase, a hydrogen peroxide-forming oxidase, from Flavobacterium meningosepticum. Appl. Environ. Microbiol. 63 (1997) 4282-4286.

[EC 1.1.3.39 created 2001]

EC 1.3.1.69

Recommended name: zeatin reductase

Reaction: dihydrozeatin + NADP = zeatin + NADPH2

Glossary:
zeatin

Systematic name: dihydrozeatin:NADP oxidoreductase

Comments: Previously classified erroneously as EC 1.1.1.242.

References:

1. Martin, R.C., Mok, M.C., Shaw, G. and Mok, D.W.S. An enzyme mediating the conversion of zeatin to dihydrozeatin in Phaseolus embryos. Plant Physiol. 90 (1989) 1630-1635.

[EC 1.3.1.69 created 1992 as EC 1.1.1.242, transferred 2001 to EC 1.3.1.69]

EC 1.14.12.18

Recommended name: biphenyl 2,3-dioxygenase

Reaction: biphenyl + NADH2 + O2 = (2R,3S)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD

For reaction pathway click here.

Other name(s): biphenyl dioxygenase

Systematic name: biphenyl,NADH2:oxygen oxidoreductase (2,3-hydroxylating)

Comments: Requires Fe2+. The enzyme from Pseudomonas sp. strain LB400 is part of a multicomponent system composed of an NADH:ferredoxin oxidoreductase (FAD cofactor), a [2Fe-2S] Rieske-type ferredoxin, and a terminal oxygenase that contains a [2Fe-2S] Rieske-type iron-sulfur cluster and a catalytic mononuclear nonheme iron centre. Chlorine-substituted biphenyls can also act as substrates. Similar to the three-component enzyme systems EC 1.14.12.3 (benzene 1,2-dioxygenase) and EC 1.14.12.11 (toluene dioxygenase).

References:

1. Haddock, J.D. and Gibson, D.T. Purification and characterization of the oxygenase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400. J. Bacteriol. 177 (1995) 5834-5839. [Medline UI: 96011369]

2. Haddock, J.D., Pelletier, D.A. and Gibson, D.T. Purification and properties of ferredoxinBPH, a component of biphenyl 2,3-dioxygenase of Pseudomonas sp. strain LB400. J. Indust. Microbiol. Biotechnol. 19 (1997) 355-359. [Medline UI: 98113813]

3. Broadus, R.M. and Haddock, J.D. Purification and characterization of the NADH:ferredoxinBPH oxidoreductase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400. Arch. Microbiol. 170 (1998) 106-112. [Medline UI: 98350019]

[EC 1.14.12.18 created 2001]

EC 1.14.15.7

Recommended name: choline monooxygenase

Reaction: choline + 2 reduced ferredoxin + O2 = betaine aldehyde + 2 oxidized ferredoxin + H2O

Glossary
betaine: N,N,N-trimethylammonioacetate
betaine aldehyde: N,N,N-trimethyl-2-oxoethylammonium
choline: (2-hydroxyethyl)trimethylammonium

Systematic name: choline,reduced-ferredoxin:oxygen oxidoreductase

Comments: Requires Mg2+ and contains a Rieske-type [2Fe-2S] cluster. Catalyses the first step of glycine betaine synthesis in plants, where it is found in the chloroplast.

References:

1. Brouquisse, R., Weigel, P., Rhodes, D., Yocum, C.F. and Hanson, A.D. Evidence for a ferredoxin-dependent choline monooxygenase from spinach chloroplast stroma. Plant Physiol. 90 (1989) 322-329.

2. Burnet, M., Lafontaine, P.J. and Hanson, A.D. Assay, purification, and partial characterization of choline monooxygenase from spinach. Plant Physiol. 108 (1995) 581-588.

3. Rathinasabapathi, B., Burnet, M., Russell, B.L., Gage, D.A., Liao, P., Nye, G.J., Scott, P., Golbeck, J.H. and Hanson, A.D. Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: Prosthetic group characterization and cDNA cloning. Proc. Natl. Acad. Sci. USA 94 (1997) 3454-3458. [Medline UI: 97250559]

4. Russell, B.L., Rathinasabapathi, B. and Hanson, A.D. Osmotic stress induces expression of choline monooxygenase in sugar beet and amaranth. Plant Physiol. 116 (1998) 859-865. [Medline UI: 98150283]

5. Nuccio, M.L., Russell, B.L., Nolte, K.D., Rathinasabapathi, B., Gage, D.A. and Hanson, A.D. The endogenous choline supply limits glycine betaine synthesis in transgenic tobacco expressing choline. Plant J. 16 (1998) 487-496. [Medline UI: 99097843]

[EC 1.14.15.7 created 2001]

EC 2.3.1.157

Recommended name: glucosamine-1-phosphate N-acetyltransferase

Reaction: acetyl-CoA + D-glucosamine 1-phosphate = CoA + N-acetyl-D-glucosamine 1-phosphate

Systematic name: acetyl-CoA:D-glucosamine-1-phosphate N-acetyltransferase

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 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase.

References:

1. 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. [Medline UI: 94364959]

[EC 2.3.1.157 created 2001]

EC 2.4.1.211

Recommended name: 1,3-β-galactosyl-N-acetylhexosamine phosphorylase

Reaction: β-D-galactopyranosyl-(1arrow right3)-N-acetyl-D-glucosamine + phosphate = α-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine

Systematic name: β-D-galactopyranosyl-(1arrow right3)-N-acetyl-D-hexosamine:phosphate galactosyltransferase

Comments: Reaction also occurs with β-D-galactopyranosyl-(1arrow right3)-N-acetyl-D-galactosamine as the substrate, giving N-acetyl-D-galactosamine as the product.

References:

1. Derensy-Dron, D., Krzewinski, F., Brassart, C. and Bouquelet S. β-1,3-Galactosyl-N-acetylhexosamine phosphorylase from Bifidobacterium bifidum DSM 20082: characterization, partial purification and relation to mucin degradation. Biotechnol. Appl. Biochem. 29 (1999) 3-10. [Medline UI: 99173770]

[EC 2.4.1.211 created 2001]

*EC 2.5.1.44

Recommended name: homospermidine synthase

Reaction: 2 putrescine = sym-homospermidine + NH3

For reaction pathway click here.

Glossary
sym-homospermidine: N-(4-aminobutyl)butane-1,4-diamine
putrescine: butane-1,4-diamine

Systematic name: putrescine:putrescine 4-aminobutyltransferase (ammonia-forming)

Comments: The reaction of this enzyme occurs in three steps: (i) NAD-dependent dehydrogenation of putrescine, (ii) transfer of the 4-aminobutylidene group from dehydroputrescine to a second molecule of putrescine, (iii) reduction of the imine intermediate to form homospermidine. Hence the overall reaction is transfer of a 4-aminobutyl group. In the presence of putrescine, spermidine can function as a donor of the aminobutyl group, in which case, propane-1,3-diamine is released instead of ammonia. Differs from EC 2.5.1.45, homospermidine synthase (spermidine-specific), which cannot use putrescine as donor of the aminobutyl group.

References:

1. Tait, G.H. The formation of homospermidine by an enzyme from Rhodopseudomonas viridis. Biochem. Soc. Trans. 7 (1979) 199-200. [Medline UI: 79170251]

2. Böttcher, F., Ober, D. and Hartmann, T. Biosynthesis of pyrrolizidine alkaloids: putrescine and spermidine are essential substrates of enzymatic homospermidine formation. Can. J. Chem. 72 (1994) 80-85.

3. Yamamoto, S., Nagata, S. and Kusaba, K. Purification and characterization of homospermidine synthase in Acinetobacter tartarogens ATCC 31105. J. Biochem. 114 (1993) 45-49. [Medline UI: 94012579]

4. Srivenugopal, K.S. and Adiga, P.R. Enzymatic synthesis of sym-homospermidine in Lathyrus sativus T (grass pea) seedlings. Biochem. J. 190 (1980) 461-464. [Medline UI: 81133501]

5. Ober, D., Tholl, D., Martin, W. and Hartmann, T. Homospermidine synthase of Rhodopseudomonas viridis: Substrate specificity and effects of the heterologously expressed enzyme on polyamine metabolism of Escherichi coli. J. Gen. Appl. Microbiol. 42 (1996) 411-419.

6. Ober, D. and Hartmann, T. Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase. Proc. Natl. Acad. Sci. USA 96 (1999) 14777-14782. [Medline UI: 20079558]

[EC 2.5.1.44 created 1999, modified 2001]

EC 2.5.1.45

Recommended name: homospermidine synthase (spermidine-specific)

Reaction: spermidine + putrescine = sym-homospermidine + propane-1,3-diamine

For reaction pathway click here.

Glossary
sym-homospermidine: N-(4-aminobutyl)butane-1,4-diamine
putrescine: butane-1,4-diamine
spermidine: N-(3-aminopropyl)butane-1,4-diamine

Systematic name: spermidine:putrescine 4-aminobutyltransferase (propane-1,3-diamine-forming)

Comments: The reaction of this enzyme occurs in three steps: (i) NAD-dependent dehydrogenation of spermidine, (ii) transfer of the 4-aminobutylidene group from dehydrospermidine to putrescine, (iii) reduction of the imine intermediate to form homospermidine. Hence the overall reaction is transfer of a 4-aminobutyl group. This enzyme is more specific than EC 2.5.1.44, homospermidine synthase, which is found in bacteria, as it cannot use putrescine as donor of the 4-aminobutyl group. Forms part of the biosynthetic pathway of the poisonous pyrrolizidine alkaloids of the ragworts (Senecio).

References:

1. Böttcher, F., Ober, D. and Hartmann, T. Biosynthesis of pyrrolizidine alkaloids: putrescine and spermidine are essential substrates of enzymatic homospermidine formation. Can. J. Chem. 72 (1994) 80-85.

2. Ober, D. and Hartmann, T. Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase. Proc. Natl. Acad. Sci. USA 96 (1999) 14777-14782. [Medline UI: 20079558]

3. Ober, D., Harms, R. and Hartmann, T. Cloning and expression of homospermidine synthase from Senecio vulgaris: a revision. Phytochemistry 55 (2000) 311-316.

[EC 2.5.1.45 created 2001]

EC 2.5.1.46

Recommended name: deoxyhypusine synthase

Reaction: [eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine

For reaction pathway click here.

Glossary
deoxyhypusine: N6-(4-aminobutyl)lysine
hypusine: N6-(4-amino-2-hydroxybutyl)lysine
spermidine: N-(3-aminopropyl)butane-1,4-diamine

Systematic name: spermidine:eIF5A-lysine 4-aminobutyltransferase (propane-1,3-diamine-forming)

Comments: The eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity. This enzyme catalyses the first reaction of hypusine formation from one specific lysine residue of the eIF5A precursor, the second reaction being catalysed by EC 1.14.99.29, deoxyhypusine monooxygenase. The reaction of this enzyme occurs in four steps: (i) NAD-dependent dehydrogenation of spermidine, (ii) formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue (Lys329 for the human enzyme), (iii) transfer of the same 4-aminobutylidene group from the enzyme intermediate to the e1F5A precursor, (iv) reduction of the e1F5A-imine intermediate to form a deoxyhypusine residue. Hence the overall reaction is transfer of a 4-aminobutyl group. For the plant enzyme, homospermidine can substitute for spermidine and putrescine can substitute for the lysine residue of the eIF5A precursor.

References:

1. Wolff, E.C., Park, M.H. and Folk, J.E. Cleavage of spermidine as the first step in deoxyhypusine synthesis. The role of NAD+. J. Biol. Chem. 265 (1990) 4793-4799. [Medline UI: 90202924]

2. Wolff, E.C., Folk, J.E. and Park, M.H. Enzyme-substrate intermediate formation at lysine 329 of human deoxyhypusine synthase. J. Biol. Chem. 272 (1997) 15865-15871. [Medline UI: 97332674]

3. Chen, K.Y. and Liu, A.Y.C. Biochemistry and function of hypusine formation on eukaryotic initiation factor 5A. Biol. Signals 6 (1997) 105-109. [Medline UI: 97430993]

4. Ober, D. and Hartmann, T. Deoxyhypusine synthase from tobacco. cDNA isolation, characterization, and bacterial expression of an enzyme with extended substrate specificity. J. Biol. Chem. 274 (1999) 32040-32047. [Medline UI: 20011401]

5. Ober, D. and Hartmann, T. Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved form deoxyhypusine synthase. Proc. Natl. Acad. Sci. USA 96 (1999) 14777-14782. [Medline UI: 20079558]

6. Wolff, E.C. and Park, M.H. Identification of lysine350 of yeast deoxyhypusine synthase as the site of enzyme intermediate formation. Yeast 15 (1999) 43-50. [Medline UI: 99152510]

7. Wolff, E.C., Wolff. J. and Park, M.H. Deoxyhypusine synthase generates and uses bound NADH in a transient hydride transfer mechanism. J. Biol. Chem. 275 (2000) 9170-9177. [Medline UI: 20200398]

8. Joe, Y.A., Wolff, E.C. and Park, M.H. Cloning and expression of human deoxyhypusine synthase cDNA: structure-function studies with the recombinant enzyme and mutant proteins. J. Biol. Chem. 270 (1995) 22386-22392. [Medline UI: 95403436]

9. Tao, Y. and Chen, K.Y. Molecular cloning and functional expression of Neurospora deoxyhypusine synthase cDNA and identification of yeast deoxyhypusine synthase cDNA. J. Biol. Chem. 270 (1995) 23984-23987. [Medline UI: 96025775]

[EC 2.5.1.46 provisional version created 1999 as EC 1.1.1.249 deleted 1999, revised and reinstated 2001 as EC 2.5.1.46]

*EC 2.6.1.37

Recommended name: 2-aminoethylphosphonate-pyruvate transaminase

Reaction: (2-aminoethyl)phosphonate + pyruvate = 2-phosphonoacetaldehyde + L-alanine

Other name(s): (2-aminoethyl)phosphonate transaminase; (2-aminoethyl)phosphonate aminotransferase; (2-aminoethyl)phosphonic acid aminotransferase; 2-aminoethylphosphonate-pyruvate aminotransferase; 2-aminoethylphosphonate aminotransferase

Systematic name: (2-aminoethyl)phosphonate:pyruvate aminotransferase

Comments: A pyridoxal-phosphate protein. 2-Aminoethylarsonate can replace 2-aminoethylphosphonate as a substrate.

References:

1. La Nauze, J.M. and Rosenberg, H. The identification of 2-phosphonoacetaldehyde as an intermediate in the degradation of 2-aminoethylphosphonate by Bacillus cereus. Biochim. Biophys. Acta 165 (1968) 438-447. [Medline UI: 70056996]

2. Dumora, C., Lacoste, A.-M. and Cassaigne, A. Purification and properties of 2-aminoethylphosphonate:pyruvate aminotransferase from Pseudomonas aeruginosa. Eur. J. Biochem. 133 (1983) 119-125. [Medline UI: 83209625]

3. Lacoste, A.-M., Dumora, C., Balas, L., Hammerschmidt, F. and Vercauteren, J. Stereochemistry of the reaction catalysed by 2-aminoethylphosphonate aminotransferase. A 1H-NMR study. Eur. J. Biochem. 215 (1993) 841-844. [Medline UI: 93358911]

4. Lacoste, A.-M., Dumora, C., Ali, B.R.S., Neuzil, E. and Dixon, H.B.F. Utilization of 2-aminoethylarsonic acid in Pseudomonas aeruginosa. J. Gen. Microbiol. 138 (1992) 1283-1287. [Medline UI: 92407501]

[EC 2.6.1.37 created 1972, modified 1982, modified 2001]

EC 2.7.1.145

Recommended name: deoxynucleoside kinase

Reaction: ATP + 2'-deoxynucleoside = ADP + 2'-deoxynucleoside 5'-phosphate

Other names: multispecific deoxynucleoside kinase; ms-dNK; multisubstrate deoxyribonculeoside kinase; multifunctional deoxynucleoside kinase; D. melanogaster deoxynucleoside kinase; Dm-dNK

Systematic name: ATP:deoxynucleoside 5'-phosphotransferase

Comments: The enzyme from embryonic cells of Drosophila melanogaster differs from other deoxynucleoside kinases [EC 2.7.1.76 (deoxyadenosine kinase) and EC 2.7.1.113 (deoxyguanosine kinase)] in its broad specificity for all four common deoxynucleosides.

References:

1. Munch-Petersen, B., Piskur, J. and Søndergaard, L. Four deoxynucleoside kinase activities from Drosophila melanogaster are contained within a single monomeric enzyme, a new multifunctional deoxynucleoside kinase. J. Biol. Chem. 273 (1998) 3926-3931. [Medline UI: 98129796]

2. Munch-Petersen, B., Knecht, W., Lenz, C., Søndergaard, L. and Piskur, J. Functional expression of a multisubstrate deoxyribonculeoside kinase from Drosophila melanogaster and its C-terminal deletion. J. Biol. Chem. 275 (2000) 6673-6679. [Medline UI: 20158988]

[EC 2.7.1.145 created 2001]

*EC 3.2.1 Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds

EC 3.2.1.145

Recommended name: galactan 1,3-β-galactosidase

Reaction: Hydrolysis of terminal, non-reducing β-D-galactose residues in (1arrow right3)-β-D-galactopyranans

Systematic name: galactan (1arrow right3)-β-D-galactosidase

Comments: This enzyme removes not only free galactose, but also 6-glycosylated residues, e.g., (1arrow right6)-β-D-galactobiose, and galactose bearing oligosaccharide chains on O-6. Hence, it releases branches from [arabino-galacto-(1arrow right6)]-(1arrow right3)-β-D-galactans.

References:

1. Tsumuraya, Y., Mochizuki, N., Hashimoto Y. and Kovac, P. Purification of exo-(1arrow right3)-D-galactanase of Irpex lacteus (Polyporus tulipiferae) and its action on arabinogalactan-proteins. J. Biol. Chem. 265 (1990) 7207-7215. [Medline UI: 90237010]

2. Pellerin, P. and Brillouet, J.M. Purification and properties of an exo-(1arrow right3)-β-D-galactanase from Aspergillus niger. Carbohydr. Res. 264 (1994) 281-291. [Medline UI: 95103561]

[EC 3.2.1.145 created 2001]

EC 3.2.1.146

Recommended name: β-galactofuranosidase

Reaction: Hydrolysis of terminal non-reducing β-D-galactofuranosides, releasing galactose.

Other name(s): exo-β-galactofuranosidase; exo-β-D-galactofuranosidase; β-D-galactofuranosidase

Systematic name: β-D-galactofuranoside hydrolase

Comments: The enzyme from Helminthosporium sacchari detoxifies helminthosporoside, a bis(digalactosyl)terpene produced by this fungus, by releasing its four molecules of bound galactose.

References:

1. Rietschel-Berst, M., Jentoft, N.H., Rick, P.D., Pletcher, C., Fang, F. and Gander, J.E. Extracellular exo-β-galactofuranosidase from Penicillium charlesii: isolation, purification, and properties. J. Biol. Chem. 252 (1977) 3219-3226. [Medline UI: 77187789]

2. Daley, L.S. and Strobel, G.A. β-Galactofuranosidase activity in Helminthosporium sacchari and its relationship to the production of helminthosporoside. Plant Sci. Lett. 30 (1983) 145-154.

3. Cousin, M.A., Notermans, S., Hoogerhout, P. and Van Boom, J.H. Detection of β-galactofuranosidase production by Penicillium and Aspergillus species using 4-nitrophenyl β-D-galactofuranoside. J. Appl. Bacteriol. 66 (1989) 311-317. [Medline UI: 89327086]

4. Miletti , L.C., Marino, C., Marino, K., de Lederkremer, R.M., Colli, W. and Alves, M.J.M. Immobilized 4-aminophenyl-1-thio-β-D-galactofuranoside as a matrix for affinity purification of an exo-β-D-galactofuranosidase. Carbohydr. Res. 320 (1999) 176-182.

[EC 3.2.1.146 created 2001]

EC 3.2.1.147

Recommended name: thioglucosidase

Reaction: H2O + a thioglucoside = a sugar + a thiol

Other name(s): myrosinase; sinigrinase; sinigrase

Systematic name: thioglucoside glucohydrolase

Comments: Has a wide specificity for thioglycosides.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9025-38-1

References:

1. Goodman, I., Fouts, J.R., Bresnick, E., Menegas, R. and Hitchings, G.H. A mammalian thioglucosidase. Science 130 (1959) 450-451.

2. Pigman, W.W. Action of almond emulsin on the phenyl glucosides of synthetic sugars and on β-thiophenyl d-glucoside. J. Res. Nat. Bur. Stand. 26 (1941) 197-204.

[EC 3.2.1.147 created 1972 as EC 3.2.3.1, transferred 2001 to EC 3.2.1.147]

EC 3.2.1.148

Recommended name: ribosylhomocysteinase

Reaction: H2O + S-ribosyl-L-homocysteine = D-ribose + L-homocysteine

Systematic name: S-ribosyl-L-homocysteine ribohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37288-63-4

References:

1. Duerre, J.A. and Miller, C.H. Cleavage of S-ribosyl-L-homocysteine by extracts from Escherichia coli. J. Bacteriol. 91 (1966) 1210-1217. [Medline UI: 66120927]

[EC 3.2.1.148 created 1972 as EC 3.3.1.3, transferred 2001 to EC 3.2.1.148]

[EC 3.2.3.1 Transferred entry: now EC 3.2.1.147 thioglucosidase (EC 3.2.3.1 created 1972, deleted 2001)]

*EC 3.3.1 Trialkylsulfonium Hydrolases

[EC 3.3.1.3 Transferred entry: now EC 3.2.1.148 ribosylhomocysteinase (EC 3.3.1.3 created 1972, deleted 2001)]

EC 3.3.2.8

Recommended name: limonene-1,2-epoxide hydrolase

Reaction: limonene-1,2-epoxide + H2O = limonene-1,2-diol

Glossary:
limonene: a monoterpenoid

Other name(s): limonene oxide hydrolase

Systematic name: limonene-1,2-epoxide hydrolase

Comment: Involved in the monoterpene degradation pathway of the actinomycete Rhodococcus erythropolis. Enzyme hydrolyses several alicyclic and 1-methyl-substituted epoxides, such as 1-methylcyclohexene oxide, indene oxide and cyclohexene oxide. It differs from the previously described epoxide hydrolases [EC 3.3.2.3 (epoxide hydrolase), EC 3.3.2.4 (trans-epoxysuccinate hydrolase), EC 3.3.2.6 (leukotriene-A4 hydrolase) and EC 3.3.2.7 (hepoxilin-epoxide hydrolase)] as it is not inhibited by 2-bromo-4'-nitroacetophenone, diethyl pyrocarbonate, 4-fluorochalcone oxide or 1,10-phenanthroline.

References:

1. van der Werf, M.J., Overkamp, K.M. and de Bont, J.A.M. Limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis DCL14 belongs to a novel class of epoxide hydrolases. J. Bacteriol. 180 (1998) 5052-5057. [Medline UI: 98422456]

2. Barbirato, F., Verdoes, J.C., de Bont, J.A.M. and van der Werf, M.J. The Rhodococcus erythropolis DCL14 limonene-1,2-epoxide hydrolase gene encodes an enzyme belonging to a novel class of epoxide hydrolases. FEBS Lett. 438 (1998) 293-296. [Medline UI: 99043266]

[EC 3.3.2.8 created 2001]

EC 3.5.2.16

Recommended name: maleimide hydrolase

Reaction: maleimide + H2O = maleamic acid

Other name(s): imidase; cyclic imide hydrolase

Systematic name: cyclic-imide amidohydrolase (decyclicizing)

Comment: Succinimide and glutarimide, and sulfur-containing cyclic imides, such as rhodanine, can also act as substrates for the enzyme from Blastobacter sp. A17p-4. The reverse, cyclization, reaction is also catalysed, but much more slowly. It has lower activity towards cyclic ureides, which are the substrates of EC 3.5.2.2, dihydropyrimidinase.

References:

1. Ogawa, J., Soong, C.L., Honda, M. and Shimizu, S. Imidase, a new dihydropyrimidinase-like enzyme involved in the metabolism of cyclic imides. Eur. J. Biochem. 243 (1997) 322-327. [Medline UI: 97182616]

[EC 3.5.2.16 created 2001]

*EC 3.11.1.1

Recommended name: phosphonoacetaldehyde hydrolase

Reaction: phosphonoacetaldehyde + H2O = acetaldehyde + phosphate

Other name(s): phosphonatase

Systematic name: 2-oxoethylphosphonate phosphonohydrolase

Comments: This enzyme destabilizes the C-P bond, by forming an imine between one of its lysine residues and the carbonyl group of the substrate, thus allowing this, normally stable, bond to be broken. The mechanism is similar to that used by EC 4.1.2.13, fructose-bisphosphate aldolase, to break a C-C bond.

References:

1. La Nauze, J.M. and Rosenberg, H. The identification of 2-phosphonoacetaldehyde as an intermediate in the degradation of 2-aminoethylphosphonate by Bacillus cereus. Biochim. Biophys. Acta 165 (1968) 438-447. [Medline UI: 70056996]

2. La Nauze, J.M., Rosenberg, H. and Shaw, D.C. The enzymic cleavage of the carbon-phosphorus bond: purification and properties of phosphonatase. Biochim. Biophys. Acta 212 (1970) 332-350. [Medline UI: 70275154]

3. La Nauze, J.M., Coggins, J.R. and Dixon, H.B.F. Aldolase-like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase. Biochem. J. 165 (1977) 409-411. [Medline UI: 78039850]

4. Olsen, D.B., Hepburn, T.W., Moos, M., Mariano, P.S. and Dunaway-Mariano, D. Substrate binding and catalytic groups of the P-C bond cleaving enzyme, phosphonoacetaldehyde hydrolase. Biochemistry 27 (1988) 2229-2234. [Medline UI: 88241058]

5. Baker, A.S., Ciocci, M.J., Metcalf, W.W., Kim, J., Babbitt, P.C., Wanner, B.L., Martin, B.M. and Dunaway-Mariano, D. Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis. Biochemistry 37 (1998) 9305-9315. [Medline UI: 98313265]

[EC 3.11.1.1 created 1972, modified 1976, modified 2001]

EC 4.2.1.100

Recommended name: cyclohexa-1,5-dienecarbonyl-CoA hydratase

Reaction: cyclohexa-1,5-dienecarbonyl-CoA + H2O = 6-hydroxycyclohex-1-enecarbonyl-CoA

Other names: cyclohexa-1,5-diene-1-carbonyl-CoA hydratase; dienoyl-CoA hydratase

Systematic name: cyclohexa-1,5-dienecarbonyl-CoA hydro-lyase

Comments: Forms part of the anaerobic benzoate degradation pathway, which also includes EC 1.3.99.7 (glutaryl-CoA dehydrogenase), EC 1.3.99.15 (benzoyl-CoA reductase) and EC 4.2.1.55 (3-hydroyxbutyryl-CoA dehydratase).

Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, WIT, CAS registry number:

References:

1. Laempe, D., Eisenreich, W., Bacher, A. and Fuchs, G. Cyclohexa-1,5-diene-1-carboxyl-CoA hydratase, an enzyme involved in anaerobic metabolism of benzoyl-CoA in the denitrifying bacterium Thauera aromatica. Eur. J. Biochem. 255 (1998) 618-627. [Medline UI: 98409281] [Erratum Eur. J. Biochem. 257 (1998) 528 only]

2. Harwood, C.S. and Gibson, J. Shedding light on anaerobic benzene ring degradation: a process unique to prokaryotes? J. Bacteriol. 179 (1997) 301-309. [Medline UI: 97144512]

3. Koch, J., Eisenreich, W., Bacher, A. and Fuchs, G. Products of enzymatic reduction of benzoyl-CoA, a key reaction in anaerobic aromatic metabolism. Eur. J. Biochem. 211 (1993) 649-661. [Medline UI: 93170297]

[EC 4.2.1.100 created 2000, modified 2001]

[EC 4.2.1.102 Transferred entry: now EC 4.2.1.100 cyclohexa-1,5-diene-1-carbonyl-CoA hydratase (EC 4.2.1.102 created 2001, deleted 2001)]

EC 5.4.2.10

Recommended name: phosphoglucosamine mutase

Reaction: D-glucosamine 1-phosphate = D-glucosamine 6-phosphate

Systematic name: D-glucosamine 1,6-phosphomutase

Comments: The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. The enzyme from E. coli is activated by phosphorylation and can be autophosphorylated in vitro by glucosamine 1,6-bisphosphate, which is an intermediate in the reaction, glucose 1,6-bisphosphate or ATP. It can also catalyse the interconversion of glucose 1-phosphate and glucose 6-phosphate, although at a much lower rate.

References:

1. Mengin-Lecreulx, D. and van Heijenoort, J. Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli. J. Biol. Chem. 271 (1996) 32-39. [Medline UI: 96132879]

2. de Reuse, H., Labigne, A. and Mengin-Lecreulx, D. The Helicobacter pylori ureC gene codes for a phosphoglucosamine mutase. J. Bacteriol. 179 (1997) 3488-3493. [Medline UI: 97315217]

3. Jolly, L., Wu, S., van Heijenoort, J., de Lencastre, H., Mengin-Lecreulx, D. and Tomas, A. The femR315 gene from Staphylococcus aureus, the interruption of which results in reduced methicillin resistance, encodes a phosphoglucosamine mutase. J. Bacteriol. 179 (1997) 5321-5325. [Medline UI: 97431478]

4. Jolly, L., Ferrari, P., Blanot, D., van Heijenoort, J., Fassy, F. and Mengin-Lecreulx, D. Reaction mechanism of phosphoglucosamine mutase from Escherichia coli. Eur. J. Biochem. 262 (1999) 202-210. [Medline UI: 99248083]

5. Jolly, L., Pompeo, F., van Heijenoort, J., Fassy, F. and Mengin-Lecreulx, D. Autophosphorylation of phosphoglucosamine mutase from Escherichia coli. J. Bacteriol. 182 (2000) 1280-1285. [Medline UI: 20138152]

[EC 5.4.2.10 created 2001]

*EC 5.5.1.4

Recommended name: inositol-3-phosphate synthase

Reaction: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate

Other name(s): myo-inositol-1-phosphate synthase

Systematic name: 1L-myo-inositol-1-phosphate lyase (isomerizing)

Comments: Requires NAD, which dehydrogenates the -CHOH- group to -CO- at C-5 of the glucose 6-phosphate, making C-6 into an active methylene, able to condense with the -CHO at C-1. Finally, the enzyme-bound NADH2 reconverts C-5 into the -CHOH- form.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9032-95-5

References:

1. Eisenberg, P., Jr. D-myo-Inositol 1-phosphate as product of cyclization of glucose 6-phosphate and substrate for a specific phosphatase in rat testis. J. Biol. Chem. 242 (1967) 1375-1382. [Medline UI: 67135042]

2. Sherman, W.R., Stewart, M.A. and Zinbo, M. Mass spectrometric study on the mechanism of D-glucose 6-phosphate-L-myo-inositol 1-phosphate cyclase. J. Biol. Chem. 244 (1969) 5703-5708. [Medline UI: 70027328]

3. Barnett, J.E.G. and Corina, D.L. The mechanism of glucose 6-phosphate-D-myo-inositol 1-phosphate cyclase of rat testis. The involvement of hydrogen atoms. Biochem. J. 108 (1968) 125-129. [Medline UI: 68310248]

4. Barnett, J.E.G., Rasheed, A. and Corina, D.L. Partial reactions of glucose 6-phosphate-1L-myo-inositol 1-phosphate cyclase. Biochem. J. 131 (1973) 21-30. [Medline UI: 73228139]

[EC 5.5.1.4 created 1972, modified 2001]


Errata

EC 1.14.12.12

The product should be (1R,2S)-1,2-dihydronaphthalene-1,2-diol [not (1S,2S)-].

EC 1.14.12.13 CO2 is also produced in the reaction.

EC 3.1.11.1-4, EC 3.1.11.6, EC 3.1.13.3, EC 3.1.15.1

The product should be nucleoside 5'-phosphates [not 5'-phosphomononucleotides].

EC 3.1.13.1

The product should be nucleoside 5'-phosphates [not 3'-phosphomononucleotides].

EC 3.1.14.1, EC 3.1.16.1, EC 3.1.22.1-2, EC 3.1.27.1, EC 3.1.27.3-6, EC 3.1.31.1

The product should be nucleoside 3'-phosphates [not 3'-phosphomononucleotides].

EC 3.6.1.31

The reaction and sytematic name change phosphoribosyl to 1-(5-phosphoribosyl).

EC 4.2.3.12

Reactant correct spelling to 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin

Systematic name correct to 2-amino-4-oxo-6-(erythro-1',2',3'-trihydroxypropyl)-7,8-dihydroxypteridine triphosphate lyase

EC 5.4.99.11

Reference 2 date corrected to 1982.


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