Enzyme Nomenclature

Continued from EC 3.1.4.1 to EC 3.1.4.51

EC 3.1.5 to EC 3.1.16

Sections

EC 3.1.5 Triphosphoric Monoester Hydrolases
EC 3.1.6 Sulfuric Ester Hydrolases
EC 3.1.7 Diphosphoric Monoester Hydrolases
EC 3.1.8 phosphoric triester hydrolases
EC 3.1.11 Exodeoxyribonucleases Producing 5'-Phosphomonoesters
EC 3.1.13 Exoribonucleases Producing 5'-Phosphomonoesters
EC 3.1.14 Exoribonucleases Producing 3'-Phosphomonoesters
EC 3.1.15 Exonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 5'-Phosphomonoesters
EC 3.1.16 Exonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 3'-Phosphomonoesters


EC 3.1.5 Triphosphoric Monoester Hydrolases

EC 3.1.5.1

Accepted name: dGTPase

Reaction: dGTP + H2O = deoxyguanosine + triphosphate

Other name(s): deoxy-GTPase; deoxyguanosine 5-triphosphate triphosphohydrolase; deoxyguanosine triphosphatase; deoxyguanosine triphosphate triphosphohydrolase

Systematic name: dGTP triphosphohydrolase

Comments: Also acts on GTP.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-63-2

References:

1. Kornberg, S.R., Lehman, I.R., Bessman, M.J., Simms, E.S. and Kornberg, A. Enzymatic cleavage of deoxyguanosine triphosphate to deoxyguanosine and tripolyphosphate. J. Biol. Chem. 233 (1958) 159-162.

[EC 3.1.5.1 created 1961]


EC 3.1.6 Sulfuric Ester Hydrolases

Contents

EC 3.1.6.1 arylsulfatase
EC 3.1.6.2 steryl-sulfatase
EC 3.1.6.3 glycosulfatase
EC 3.1.6.4 N-acetylgalactosamine-6-sulfatase
EC 3.1.6.5 deleted
EC 3.1.6.6 choline-sulfatase
EC 3.1.6.7 cellulose-polysulfatase
EC 3.1.6.8 cerebroside-sulfatase
EC 3.1.6.9 chondro-4-sulfatase
EC 3.1.6.10 chondro-6-sulfatase
EC 3.1.6.11 disulfoglucosamine-6-sulfatase
EC 3.1.6.12 N-acetylgalactosamine-4-sulfatase
EC 3.1.6.13 iduronate-2-sulfatase
EC 3.1.6.14 N-acetylglucosamine-6-sulfatase
EC 3.1.6.15 N-sulfoglucosamine-3-sulfatase
EC 3.1.6.16 monomethyl-sulfatase
EC 3.1.6.17 D-lactate-2-sulfatase
EC 3.1.6.18 glucuronate-2-sulfatase
EC 3.1.6.19 (R)-specific secondary-alkylsulfatase
EC 3.1.6.20 S-sulfosulfanyl-L-cysteine sulfohydrolase


Entries

EC 3.1.6.1

Accepted name: arylsulfatase

Reaction: A phenol sulfate + H2O = a phenol + sulfate

Other name(s): sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase

Systematic name: aryl-sulfate sulfohydrolase

Comments: A group of enzymes with rather similar specificities.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9016-17-5

References:

1. Dodgson, K.S., Spencer, B. and Williams, K. Studies on sulphatases. 13. The hydrolysis of substituted phenyl sulphates by the arylsulphatase of Alcaligenes metacaligenes. Biochem. J. 64 (1956) 216-221.

2. Roy, A.B. The synthesis and hydrolysis of sulfate esters. Adv. Enzymol. Relat. Subj. Biochem. 22 (1960) 205-235.

3. Roy, A.B. Sulphatases, lysosomes and disease. Aust. J. Exp. Biol. Med. Sci. 54 (1976) 111-135. [PMID: 13772]

4. Webb, E.C. and Morrow, P.F.W. The activation of an arysulphatase from ox liver by chloride and other anions. Biochem. J. 73 (1959) 7-15.

[EC 3.1.6.1 created 1961]

EC 3.1.6.2

Accepted name: steryl-sulfatase

Reaction: 3β-hydroxyandrost-5-en-17-one 3-sulfate + H2O = 3β-hydroxyandrost-5-en-17-one + sulfate

Other name(s): arylsulfatase; steroid sulfatase; sterol sulfatase; dehydroepiandrosterone sulfate sulfatase; arylsulfatase C; steroid 3-sulfatase; steroid sulfate sulfohydrolase; dehydroepiandrosterone sulfatase; pregnenolone sulfatase; phenolic steroid sulfatase; 3-β-hydroxysteroid sulfate sulfatase

Systematic name: steryl-sulfate sulfohydrolase

Comments: Also acts on some related steryl sulfates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-62-1

References:

1. Roy, A.B. The steroid sulphatase of Patella vlugata. Biochim. Biophys. Acta 15 (1954) 300-301.

2. Roy, A.B. The synthesis and hydrolysis of sulfate esters. Adv. Enzymol. Relat. Subj. Biochem. 22 (1960) 205-235.

3. Stitch, S.R., Halkerston, I.D.K. and Hillman, J. The enzymic hydrolysis of steroid conjugates. 1. Sulphatase and β-glucuronidase activity of molluscan extracts. Biochem. J. 63 (1965) 705-710.

[EC 3.1.6.2 created 1961]

EC 3.1.6.3

Accepted name: glycosulfatase

Reaction: D-glucose 6-sulfate + H2O = D-glucose + sulfate

Other name(s): glucosulfatase

Systematic name: sugar-sulfate sulfohydrolase

Comments: Also acts on other sulfates of monosaccharides and disaccharides and on adenosine 5'-sulfate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9025-61-0

References:

1. Dodgson, K.S. Glycosulphatase: observations on the activity of partially purified preparations towards the sulphate esters of certain monosaccharides and steroids. Biochem. J. 78 (1961) 324-333.

2. Egami, F. and Takahaski, N. Syntheses of adenosinesulfuric acids. Bull. Chem. Soc. Jpn. 28 (1955) 666-668.

3. Roy, A.B. The synthesis and hydrolysis of sulfate esters. Adv. Enzymol. Relat. Subj. Biochem. 22 (1960) 205-235.

[EC 3.1.6.3 created 1961]

EC 3.1.6.4

Accepted name: N-acetylgalactosamine-6-sulfatase

Reaction: Hydrolysis of the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of chondroitin sulfate and of the D-galactose 6-sulfate units of keratan sulfate

For diagram click here.

Other name(s): chondroitin sulfatase; chondroitinase; galactose-6-sulfate sulfatase; acetylgalactosamine 6-sulfatase; N-acetylgalactosamine-6-sulfate sulfatase; N-acetylgalactosamine 6-sulfatase

Systematic name: N-acetyl-D-galactosamine-6-sulfate 6-sulfohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-60-9

References:

1. Epstein, E.H. and Leventhal, M.E. Steroid sulfatase of human leukocytes and epidermis and the diagnosis of recessive X-linked ichthyosis. J. Clin. Invest. 67 (1981) 1257-1262. [PMID: 6939689]

2. Glössl, J. and Kresse, H. Impaired degradation of keratan sulphate by Morquio A fibroblasts. Biochem. J. 203 (1982) 335-338. [PMID: 6213226]

3. Lim, C.T. and Horwitz, A.L. Purification and properties of human N-acetylgalactosamine-6-sulfate sulfatase. Biochim. Biophys. Acta 657 (1981) 344-355. [PMID: 7213753]

4. Sørensen, S.H., Norén, O., Sjöström, H. and Danielsen, E.M. Amphiphilic pig intestinal microvillus maltase/glucoamylase. Structure and specificity. Eur. J. Biochem. 126 (1982) 559-568. [PMID: 6814909]

5. Yutaka, T., Okada, S., Kato, T., Inui, K. and Yabuchi, H. Galactose 6-sulfate sulfatase activity in Morquio syndrome. Clin. Chim. Acta 122 (1982) 169-180. [PMID: 6809361]

[EC 3.1.6.4 created 1961]

[EC 3.1.6.5 Deleted entry: sinigrin sulfohydrolase; myrosulfatase (EC 3.1.6.5 created 1961, deleted 1964)]

EC 3.1.6.6

Accepted name: choline-sulfatase

Reaction: choline sulfate + H2O = choline + sulfate

Systematic name: choline-sulfate sulfohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9025-59-6

References:

1. Takebe, I. Isolation and characterization of a new enzyme choline sulfatase. J. Biochem. (Tokyo) 50 (1961) 245-255.

[EC 3.1.6.6 created 1965]

EC 3.1.6.7

Accepted name: cellulose-polysulfatase

Reaction: Hydrolysis of the 2- and 3-sulfate groups of the polysulfates of cellulose and charonin

Systematic name: cellulose-sulfate sulfohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9025-58-5

References:

1. Takahashi, N. and Egami, F. Hydrolysis of polysaccharide sulphate esters by a sulphatase preparation from Charonia lampas. Biochem. J. 80 (1961) 384-386.

[EC 3.1.6.7 created 1965]

EC 3.1.6.8

Accepted name: cerebroside-sulfatase

Reaction: A cerebroside 3-sulfate + H2O = a cerebroside + sulfate

Other name(s): arylsulfatase A; cerebroside sulfate sulfatase

Systematic name: cerebroside-3-sulfate 3-sulfohydrolase

Comments: Hydrolyses galactose-3-sulfate residues in a number of lipids. Also hydrolyses ascorbate 2-sulfate and many phenol sulfates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9068-68-2

References:

1. Mehl, E. and Jatzkewitz, H. A cerebrosidesulfatase from swine kidney. Hoppe-Seyler's Z. Physiol. Chem. 339 (1964) 260-276. [PMID: 5829234]

2. Roy, A.B. Sulphatases, lysosomes and disease. Aust. J. Exp. Biol. Med. Sci. 54 (1976) 111-135. [PMID: 13772]

[EC 3.1.6.8 created 1972]

EC 3.1.6.9

Accepted name: chondro-4-sulfatase

Reaction: 4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine 4-sulfate + H2O = 4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine + sulfate

Other name(s): chondroitin-4-sulfatase; 4-deoxy-β-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine-4-sulfate 4-sulfohydrolase

Systematic name: 4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine-4-sulfate 4-sulfohydrolase

Comments: Also acts on the saturated analogue but not on higher oligosaccharides, nor any 6-sulfates.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9045-75-4

References:

1. Held, V.E. and Buddecke, E. Nachweis, Reinigung und Eigenschaften einer Chondroitin-4-Sulfatase aus der Aorta des Rindes. Hoppe-Seyler's Z. Physiol. Chem. 348 (1967) 1047-1060. [PMID: 5595107]

2. Roy, A.B. Sulphatases, lysosomes and disease. Aust. J. Exp. Biol. Med. Sci. 54 (1976) 111-135. [PMID: 13772]

3. Yamagata, T., Saito, H., Habuchi, O. and Suzuki, S. Purification and properties of bacterial chondroitinases and chondrosulfatases. J. Biol. Chem. 243 (1968) 1523-1235. [PMID: 5647268]

[EC 3.1.6.9 created 1972]

EC 3.1.6.10

Accepted name: chondro-6-sulfatase

Reaction: 4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine 6-sulfate + H2O = 4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine + sulfate

Other name(s): 4-deoxy-β-D-gluc-4-enuronosyl-(1,3)-N-acetyl-D-galactosamine-6-sulfate 6-sulfohydrolase

Systematic name: 4-deoxy-β-D-gluc-4-enuronosyl-(1→3)-N-acetyl-D-galactosamine-6-sulfate 6-sulfohydrolase

Comments: Also acts on the saturated analogue and N-acetyl-D-galactosamine 4,6-disulfate, but not higher oligosaccharides, nor any 4-sulfate

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9045-76-5

References:

1. Yamagata, T., Saito, H., Habuchi, O. and Suzuki, S. Purification and properties of bacterial chondroitinases and chondrosulfatases. J. Biol. Chem. 243 (1968) 1523-1535. [PMID: 5647268]

[EC 3.1.6.10 created 1972]

EC 3.1.6.11

Accepted name: disulfoglucosamine-6-sulfatase

Reaction: 2-N,6-O-disulfo-D-glucosamine + H2O = 2-N-sulfo-D-glucosamine + sulfate

Other name(s): N-sulfoglucosamine-6-sulfatase; 6,N-disulfoglucosamine 6-O-sulfohydrolase; N,6-O-disulfo-D-glucosamine 6-sulfohydrolase

Systematic name: 2-N,6-O-disulfo-D-glucosamine 6-sulfohydrolase

Comments: May be identical with EC 3.1.6.14 N-acetylglucosamine-6-sulfatase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37288-32-7

References:

1. Dietrich, C.P. Enzymic degradation of heparin. A sulphamidase and a sulphoesterase from Flavobacterium heparinum. Biochem. J. 111 (1969) 91-95. [PMID: 5775690]

[EC 3.1.6.11 created 1972, modified 1989]

EC 3.1.6.12

Accepted name: N-acetylgalactosamine-4-sulfatase

Reaction: Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate

For diagram click here.

Other name(s): chondroitinsulfatase; chondroitinase; arylsulfatase B; acetylgalactosamine 4-sulfatase; N-acetylgalactosamine 4-sulfate sulfohydrolase

Systematic name: N-acetyl-D-galactosamine-4-sulfate 4-sulfohydrolase

Comments: Acts also on N-acetylglucosamine 4-sulfate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 55354-43-3

References:

1. Farooqui, A.A. The desulphation of hexosamine sulphates by arylsulphatase B. Experientia 32 (1976) 1242-1244. [PMID: 976430]

2. Gorham, S.D. and Cantz, M. Arylsulphatase B, an exo-sulphatase for chondroitin 4-sulphate tetrasaccharide. Hoppe-Seyler's Z. Physiol. Chem. 359 (1978) 1811-1814. [PMID: 738706]

3. Tsuji, M., Nakanishi, Y., Habuchi, H., Ishihara, K. and Suzuki, S. The common identity of UDP-N-acetylgalactosamine 4-sulfatase, nitrocatechol sulfatase (arylsulfatase), and chondroitin 4-sulfatase. Biochim. Biophys. Acta 612 (1980) 373-383. [PMID: 7370276]

[EC 3.1.6.12 created 1984]

EC 3.1.6.13

Accepted name: iduronate-2-sulfatase

Reaction: Hydrolysis of the 2-sulfate groups of the L-iduronate 2-sulfate units of dermatan sulfate, heparan sulfate and heparin

Other name(s): chondroitinsulfatase; idurono-2-sulfatase; iduronide-2-sulfate sulfatase; L-iduronosulfatase; L-idurono sulfate sulfatase; iduronate sulfatase; sulfo-L-iduronate sulfatase; L-iduronate 2-sulfate sulfatase; sulfoiduronate sulfohydrolase; 2-sulfo-L-iduronate 2-sulfatase; iduronate-2-sulfate sulfatase; iduronate sulfate sulfatase

Systematic name: L-iduronate-2-sulfate 2-sulfohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 50936-59-9

References:

1. Archer, I.M., Harper, P.S. and Wusteman, F.S. Multiple forms of iduronate 2-sulphate sulphatase in human tissues and body fluids. Biochim. Biophys. Acta 708 (1982) 134-140. [PMID: 6816283]

2. Bach, J., Eisenberg, F., Cantz, M. and Neufeld, E.C. The defect in the Hunter syndrome: deficiency of sulfoiduronate sulfatase. Proc. Natl. Acad. Sci. USA 70 (1973) 2134-2138. [PMID: 4269173]

3. DiNatale, P. and Ronsivalle, L. Identification and partial characterization of two enzyme forms of iduronate sulfatase from human placenta. Biochim. Biophys. Acta 661 (1981) 106-111. [PMID: 6945876]

4. Yutaka, T., Fluharty, A.L., Stevens, R.L. and Kihara, H. Purification and some properties of human liver iduronate sulfatase. J. Biochem. (Tokyo) 91 (1982) 433-441. [PMID: 6950934]

[EC 3.1.6.13 created 1984]

EC 3.1.6.14

Accepted name: N-acetylglucosamine-6-sulfatase

Reaction: Hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate

Other name(s): chondroitinsulfatase; O,N-disulfate O-sulfohydrolase; acetylglucosamine 6-sulfatase; N-acetylglucosamine 6-sulfate sulfatase; acetylglucosamine 6-sulfatase; 2-acetamido-2-deoxy-D-glucose 6-sulfate sulfatase

Systematic name: N-acetyl-D-glucosamine-6-sulfate 6-sulfohydrolase

Comments: May be identical with EC 3.1.6.11 disulfoglucosamine-6-sulfatase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 65666-34-4

References:

1. Basner, R., Kresse, H. and von Figura, K. N-Acetylglucosamine-6-sulfate sulfatase from human urine. J. Biol. Chem. 254 (1979) 1151-1158. [PMID: 762121]

2. Kresse, H., Fuchs, W., Glössl, J., Holtfrerich, D. and Gilberg, W. Liberation of N-acetylglucosamine-6-sulfate by human β-N-acetylhexosaminidase A. J. Biol. Chem. 256 (1981) 12926-12932. [PMID: 6458607]

3. Weissmann, B., Chao, H. and Chow, P. A glucosamine O,N-disulfate O-sulfohydrolase with a probable role in mammalian catabolism of heparan sulfate. Biochem. Biophys. Res. Commun. 97 (1980) 827-833. [PMID: 6451222]

[EC 3.1.6.14 created 1984]

EC 3.1.6.15

Accepted name: N-sulfoglucosamine-3-sulfatase

Reaction: Hydrolysis of the 3-sulfate groups of the N-sulfo-D-glucosamine 3-O-sulfate units of heparin

Other name(s): chondroitinsulfatase

Systematic name: N-sulfo-3-sulfoglucosamine 3-sulfohydrolase

Comments: The enzyme from Flavobacterium heparinum also hydrolyses N-acetyl-D-glucosamine 3-O-sulfate; the mammalian enzyme acts only on the disulfated residue.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Bruce, J.S., McLean, M.W., Long, W.F. and Williamson, F.B. Flavobacterium heparinum 3-O-sulphatase for N-substituted glucosamine 3-O-sulphate. Eur. J. Biochem. 148 (1985) 359-365. [PMID: 3987694]

2. Leder, I.G. A novel 3-O sulfatase from human urine acting on methyl-2-deoxy-2-sulfamino-α-D-glucopyranoside 3-sulfate. Biochem. Biophys. Res. Commun. 94 (1980) 1183-1189. [PMID: 7396957]

[EC 3.1.6.15 created 1984, modified 1989]

EC 3.1.6.16

Accepted name: monomethyl-sulfatase

Reaction: monomethyl sulfate + H2O = methanol + sulfate

Systematic name: monomethyl-sulfate sulfohydrolase

Comments: Highly specific; does not act on monoethyl sulfate, monoisopropyl sulfate or monododecyl sulfate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Ghisalba, O. and Küenzi, M. Biodegradation and utilization of monomethyl sulfate by specialized methylotrophs. Experientia 39 (1983) 1257-1263. [PMID: 6641899]

[EC 3.1.6.16 created 1989]

EC 3.1.6.17

Accepted name: D-lactate-2-sulfatase

Reaction: (R)-2-O-sulfolactate + H2O = (R)-lactate + sulfate

Systematic name: (R)-2-O-sulfolactate 2-sulfohydrolase

Comments: Highly specific.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 93586-05-1

References:

1. Crescenzi, A.M.V., Dodgson, K.S. and White, G.F. Purification and some properties of the D-lactate-2-sulphatase of Pseudomonas syringae GG. Biochem. J. 223 (1984) 487-494. [PMID: 6497859]

[EC 3.1.6.17 created 1989]

EC 3.1.6.18

Accepted name: glucuronate-2-sulfatase

Reaction: Hydrolysis of the 2-sulfate groups of the 2-O-sulfo-D-glucuronate residues of chondroitin sulfate, heparin and heparitin sulfate

Other name(s): glucurono-2-sulfatase

Systematic name: polysaccharide-2-O-sulfo-D-glucuronate 2-sulfohydrolase

Comments: Does not act on iduronate 2-sulfate residues (cf. EC 3.1.6.13 iduronate-2-sulfatase)

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 98597-45-6

References:

1. Shaklee, P.N., Glaser, J.H. and Conrad, H.E. A sulfatase specific for glucuronic acid 2-sulfate residues in glycosaminoglycans. J. Biol. Chem. 260 (1985) 9146-9149. [PMID: 4019466]

[EC 3.1.6.18 created 1989]

EC 3.1.6.19

Accepted name: (R)-specific secondary-alkylsulfatase

Reaction: an (R)-secondary-alkyl sulfate + H2O = an (S)-secondary-alcohol + sulfate

Other name(s): S3 secondary alkylsulphohydrolase; Pisa1; secondary alkylsulphohydrolase; (R)-specific sec-alkylsulfatase; sec-alkylsulfatase

Systematic name: (R)-secondary-alkyl sulfate sulfohydrolase [(S)-secondary-alcohol forming]

Comments: The enzyme from Rhodococcus ruber is involved in the biodegradation of alkyl sulfate esters used as detergents and released into the environment. The prefered substrates are linear secondary-alkyl sulfate esters, particularly octan-2-yl, octan-3-yl, and octan-4-yl sulfates [1]. The enzyme from Pseudomonas sp. DSM6611 utilizes a range of secondary-alkyl sulfate esters bearing aromatic, olefinic and acetylenic moieties. Perfect enantioselectivities are obtained for substrates bearing groups of different size adjacent to the sulfate moiety [4]. The enzymatic hydrolysis proceeds through inversion of the configuration at the stereogenic carbon atom [1,4]. The enzyme contains a Zn2+ ion [3].

Links to other databases: BRENDA, EXPASY, GTD, KEGG, CAS registry number:

References:

1. Pogorevc, M. and Faber, K. Purification and characterization of an inverting stereo- and enantioselective sec-alkylsulfatase from the gram-positive bacterium Rhodococcus ruber DSM 44541. Appl. Environ. Microbiol. 69 (2003) 2810-2815. [PMID: 12732552]

2. Wallner, S.R., Nestl, B.M. and Faber, K. Highly enantioselective sec-alkyl sulfatase activity of Sulfolobus acidocaldarius DSM 639. Org. Lett. 6 (2004) 5009-5010. [PMID: 15606122]

3. Knaus, T., Schober, M., Kepplinger, B., Faccinelli, M., Pitzer, J., Faber, K., Macheroux, P. and Wagner, U. Structure and mechanism of an inverting alkylsulfatase from Pseudomonas sp. DSM6611 specific for secondary alkyl sulfates. FEBS J. 279 (2012) 4374-4384. [PMID: 23061549]

4. Schober, M., Knaus, T., Toesch, M., Macheroux, P., Wagner, U. and Faber, K. The substrate spectrum of the inverting sec-alkylsulfatase Pisa1. Adv. Synth. Catal. 354 (2012) 1737-1742.

[EC 3.1.6.19 created 2013]

EC 3.1.6.20

Accepted name: S-sulfosulfanyl-L-cysteine sulfohydrolase

Reaction: (1) [SoxY protein]-S-sulfosulfanyl-L-cysteine + H2O = [SoxY protein]-S-sulfanyl-L-cysteine + sulfate
(2) [SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + H2O = [SoxY protein]-S-disulfanyl-L-cysteine + sulfate

Other name(s): SoxB

Systematic name: [SoxY protein]-S-sulfosulfanyl-L-cysteine sulfohydrolase

Comments: Contains Mn2+. The enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate. It catalyses two reactions in the pathway. In both cases the enzyme hydrolyses a sulfonate moiety that is bound (either directly or via a sulfane) to a cysteine residue of a SoxY protein, releasing sulfate. The enzyme from Paracoccus pantotrophus contains a pyroglutamate (cycloglutamate) at its N-terminus.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Quentmeier, A. and Friedrich, C.G. The cysteine residue of the SoxY protein as the active site of protein-bound sulfur oxidation of Paracoccus pantotrophus GB17. FEBS Lett. 503 (2001) 168-172. [PMID: 11513876]

2. Friedrich, C.G., Rother, D., Bardischewsky, F., Quentmeier, A. and Fischer, J. Oxidation of reduced inorganic sulfur compounds by bacteria: emergence of a common mechanism. Appl. Environ. Microbiol. 67 (2001) 2873-2882. [PMID: 11425697]

3. Quentmeier, A., Hellwig, P., Bardischewsky, F., Grelle, G., Kraft, R. and Friedrich, C.G. Sulfur oxidation in Paracoccus pantotrophus: interaction of the sulfur-binding protein SoxYZ with the dimanganese SoxB protein. Biochem. Biophys. Res. Commun. 312 (2003) 1011-1018. [PMID: 14651972]

4. Epel, B., Schafer, K.O., Quentmeier, A., Friedrich, C. and Lubitz, W. Multifrequency EPR analysis of the dimanganese cluster of the putative sulfate thiohydrolase SoxB of Paracoccus pantotrophus. J. Biol. Inorg. Chem. 10 (2005) 636-642. [PMID: 16133204]

5. Hensen, D., Sperling, D., Truper, H.G., Brune, D.C. and Dahl, C. Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum. Mol. Microbiol. 62 (2006) 794-810. [PMID: 16995898]

6. Grabarczyk, D.B. and Berks, B.C. Intermediates in the Sox sulfur oxidation pathway are bound to a sulfane conjugate of the carrier protein SoxYZ. PLoS One 12 (2017) e0173395. [PMID: 28257465]

[EC 3.1.6.20 created 2018]


EC 3.1.7 Diphosphoric Monoester Hydrolases

Contents

EC 3.1.7.1 prenyl-diphosphatase
EC 3.1.7.2 guanosine-3',5'-bis(diphosphate) 3'-diphosphatase
EC 3.1.7.3 monoterpenyl-diphosphatase
EC 3.1.7.4 deleted, now covered by EC 4.2.1.133 and EC 4.2.3.141
EC 3.1.7.5 geranylgeranyl diphosphate diphosphatase
EC 3.1.7.6 farnesyl diphosphatase
EC 3.1.7.7 transferred now EC 4.2.3.194
EC 3.1.7.8 tuberculosinol synthase
EC 3.1.7.9 isotuberculosinol synthase
EC 3.1.7.10 (13E)-labda-7,13-dien-15-ol synthase
EC 3.1.7.11 geranyl diphosphate diphosphatase
EC 3.1.7.12 (+)-kolavelool synthase


Entries

EC 3.1.7.1

Accepted name: prenyl-diphosphatase

Reaction: prenyl diphosphate + H2O = prenol + diphosphate

Other name(s): prenyl-pyrophosphatase; prenol pyrophosphatase; prenylphosphatase

Systematic name: prenyl-diphosphate diphosphohydrolase

Comments: Farnesyl diphosphate is the best substrate tested to date.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37288-33-8

References:

1. Tsai, S.-C. and Gaylor, J.L. Testicular sterols. V. Preparation and partial purification of a microsomal prenol pyrophosphate pyrophosphohydrolase. J. Biol. Chem. 241 (1966) 4043-4050. [PMID: 4288361]

[EC 3.1.7.1 created 1972]

EC 3.1.7.2

Accepted name: guanosine-3',5'-bis(diphosphate) 3'-diphosphatase

Reaction: guanosine 3',5'-bis(diphosphate) + H2O = GDP + diphosphate

Glossary: GDP = guanosine 5'-diphosphate

Other name(s): guanosine-3',5'-bis(diphosphate) 3'-pyrophosphatase; PpGpp-3'-pyrophosphohydrolase; PpGpp phosphohydrolase

Systematic name: guanosine-3',5'-bis(diphosphate) 3'-diphosphohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 70457-12-4

References:

1. Heinemeyer, E.-A. and Richter, D. Characterization of the guanosine 5'-triphosphate 3'-diphosphate and guanosine 5'-diphosphate 3'-diphosphate degradation reaction catalyzed by a specific pyrophosphorylase from Escherichia coli. Biochemistry 17 (1978) 5368-5372. [PMID: 365225]

2. Richter, D., Fehr, S. and Harder, R. The guanosine 3',5'-bis(diphosphate) (ppGpp) cycle. Comparison of synthesis and degradation of guanosine 3',5'-bis(diphosphate) in various bacterial systems. Eur. J. Biochem. 99 (1979) 57-64. [PMID: 114395]

[EC 3.1.7.2 created 1980]

EC 3.1.7.3

Accepted name: monoterpenyl-diphosphatase

Reaction: a monoterpenyl diphosphate + H2O = a monoterpenol + diphosphate

For diagram click here.

Other name(s): bornyl pyrophosphate hydrolase; monoterpenyl-pyrophosphatase

Systematic name: monoterpenyl-diphosphate diphosphohydrolase

Comments: A group of enzymes with varying specificity for the monoterpenol moiety. One has the highest activity on sterically hindered compounds such as (+)-bornyl diphosphate; another has highest activity on the diphosphates of primary allylic alcohols such as geraniol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Croteau, R. and Karp, F. Biosynthesis of monoterpenes: hydrolysis of bornyl pyrophosphate, an essential step in camphor biosynthesis, and hydrolysis of geranyl pyrophosphate, the acyclic precursor of camphor, by enzymes from sage (Salvia officinalis). Arch. Biochem. Biophys. 198 (1979) 523-532. [PMID: 42357]

[EC 3.1.7.3 created 1984]

[EC 3.1.7.4 Deleted entry: Now recognized as two enzymes EC 4.2.1.133, copal-8-ol diphosphate synthase and EC 4.2.3.141 sclareol synthase (EC 3.1.7.4 created 2008, deleted 2013)]

EC 3.1.7.5

Accepted name: geranylgeranyl diphosphate diphosphatase

Reaction: geranylgeranyl diphosphate + H2O = geranylgeraniol + diphosphate

For diagram click here.

glossary: plaunotol = 18-hydroxygeranylgeraniol

Other name(s): geranylgeranyl diphosphate phosphatase

Systematic name: geranyl-diphosphate diphosphohydrolase

Comments: Involved in the biosynthesis of plaunotol. There are two isoenzymes with different ion requirements. Neither require Mg2+ but in addition PII is inhibited by Zn2+, Mn2+ and Co2+. It is not known which isoenzyme is involved in plaunotol biosynthesis.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Nualkaew, N., De-Eknamkul, W., Kutchan, T.M. and Zenk, M.H. Membrane-bound geranylgeranyl diphosphate phosphatases: purification and characterization from Croton stellatopilosus leaves. Phytochemistry 67 (2006) 1613-1620. [PMID: 16445953]

[EC 3.1.7.5 created 2009]

EC 3.1.7.6

Accepted name: farnesyl diphosphatase

Reaction: (2E,6E)-farnesyl diphosphate + H2O = (2E,6E)-farnesol + diphosphate

For diagram of reaction click here.

Other name(s): FPP phosphatase

Systematic name: (2E,6E)-farnesyl-diphosphate diphosphohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Song, L. A soluble form of phosphatase in Saccharomyces cerevisiae capable of converting farnesyl diphosphate into E,E-farnesol. Appl. Biochem. Biotechnol. 128 (2006) 149-158. [PMID: 16484724]

2. Tsai, S.-C. and Gaylor, J.L. Testicular sterols. V. Preparation and partial purification of a microsomal prenol pyrophosphate pyrophosphohydrolase. J. Biol. Chem. 241 (1966) 4043-4050. [PMID: 4288361]

[EC 3.1.7.6 created 2010]

[EC 3.1.7.7 Transferred entry: (–)-drimenol synthase. Now EC 4.2.3.194, (–)-drimenol synthase (EC 3.1.7.7 created 2011, deleted 2017)]

EC 3.1.7.8

Accepted name: tuberculosinol synthase

Reaction: tuberculosinyl diphosphate + H2O = tuberculosinol + diphosphate

For diagram of reaction click here.

Glossary: tuberculosinyl diphosphate = halima-5,13-dien-15-yl diphosphate

Other name(s): Rv3378c

Systematic name: tuberculosinyl diphosphate diphosphohydrolase (tuberculosinol forming)

Comments: Only found in species of Mycobacterium that cause tuberculosis. In addition, it also gives isotuberculosinol in 1:1 mixture, cf EC 3.1.7.9, isotuberculosinol synthase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Nakano, C., Ootsuka, T., Takayama, K., Mitsui, T., Sato, T. and Hoshino, T. Characterization of the Rv3378c gene product, a new diterpene synthase for producing tuberculosinol and (13R,S)-isotuberculosinol (nosyberkol), from the Mycobacterium tuberculosis H37Rv genome. Biosci. Biotechnol. Biochem. 75 (2011) 75-81. [PMID: 21228491]

2. Hoshino, T., Nakano, C., Ootsuka, T., Shinohara, Y. and Hara, T. Substrate specificity of Rv3378c, an enzyme from Mycobacterium tuberculosis, and the inhibitory activity of the bicyclic diterpenoids against macrophage phagocytosis. Org. Biomol. Chem. 9 (2011) 2156-2165. [PMID: 21290071]

[EC 3.1.7.8 created 2011]

EC 3.1.7.9

Accepted name: isotuberculosinol synthase

Reaction: tuberculosinyl diphosphate + H2O = (13S)-isotuberculosinol + diphosphate

For diagram of reaction click here.

Glossary: tuberculosinyl diphosphate = halima-5,13-dien-15-yl diphosphate

Other name(s): Rv3378c

Systematic name: tuberculosinyl diphosphate diphosphohydrolase (isotuberculosinol forming)

Comments: Only found in species of Mycobacterium that cause tuberculosis. In addition, it also gives tuberculosinol in 1:1 mixture, cf EC 3.1.7.8, tuberculosinol synthase. The isotuberculosinol form was a 3:1 mixture of the 13S and1 3R forms, respectively.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Nakano, C., Ootsuka, T., Takayama, K., Mitsui, T., Sato, T. and Hoshino, T. Characterization of the Rv3378c gene product, a new diterpene synthase for producing tuberculosinol and (13R,S)-isotuberculosinol (nosyberkol), from the Mycobacterium tuberculosis H37Rv genome. Biosci. Biotechnol. Biochem. 75 (2011) 75-81. [PMID: 21228491]

2. Hoshino, T., Nakano, C., Ootsuka, T., Shinohara, Y. and Hara, T. Substrate specificity of Rv3378c, an enzyme from Mycobacterium tuberculosis, and the inhibitory activity of the bicyclic diterpenoids against macrophage phagocytosis. Org. Biomol. Chem. 9 (2011) 2156-2165. [PMID: 21290071]

[EC 3.1.7.9 created 2011]

EC 3.1.7.10

Accepted name: (13E)-labda-7,13-dien-15-ol synthase

Reaction: geranylgeranyl diphosphate + H2O = (13E)-labda-7,13-dien-15-ol + diphosphate

For diagram of reaction click here and mechanism click here.

Other name(s): labda-7,13E-dien-15-ol synthase

Systematic name: geranylgeranyl-diphosphate diphosphohydrolase [(13E)-labda-7,13-dien-15-ol-forming]

Comments: The enzyme from the lycophyte Selaginella moellendorffii is bifunctional, initially forming (13E)-labda-7,13-dien-15-yl diphosphate, which is hydrolysed to the alcohol.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Mafu, S., Hillwig, M.L. and Peters, R.J. A novel labda-7,13E-dien-15-ol-producing bifunctional diterpene synthase from Selaginella moellendorffii. Chembiochem. 12 (2011) 1984-1987. [PMID: 21751328]

[EC 3.1.7.10 created 2012]

EC 3.1.7.11

Accepted name: geranyl diphosphate diphosphatase

Reaction: geranyl diphosphate + H2O = geraniol + diphosphate

For diagram of reaction click here.

Other name(s): geraniol synthase; geranyl pyrophosphate pyrophosphatase; GES; CtGES

Systematic name: geranyl-diphosphate diphosphohydrolase

Comments: Isolated from Ocimum basilicum (basil) and Cinnamomum tenuipile (camphor tree). Requires Mg2+ or Mn2+. Geraniol is labelled when formed in the presence of [18O]H2O. Thus mechanism involves a geranyl cation [1]. Neryl diphosphate is hydrolysed more slowly. May be the same as EC 3.1.7.3 monoterpenyl-diphosphatase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Iijima, Y., Gang, D.R., Fridman, E., Lewinsohn, E. and Pichersky, E. Characterization of geraniol synthase from the peltate glands of sweet basil. Plant Physiol. 134 (2004) 370-379. [PMID: 14657409]

2. Yang, T., Li, J., Wang, H.X. and Zeng, Y. A geraniol-synthase gene from Cinnamomum tenuipilum. Phytochemistry 66 (2005) 285-293. [PMID: 15680985]

[EC 3.1.7.11 created 2012]

EC 3.1.7.12

Accepted name: (+)-kolavelool synthase

Reaction: (+)-kolavenyl diphosphate + H2O = (+)-kolavelool + diphosphate

For diagram of reaction click here

Glossary: (+)-kolavelool = (2ξ)-3-methyl-5-[(1R,2S,4aS,8aS)-1,2,4a,5-tetramethyl-1,2,3,4,4a,7,8,8a-octahydronaphthalen-1-yl]pent-1-en-3-ol

Other name(s): Haur_2146

Systematic name: kolavenyl-diphosphate diphosphohydrolase

Comments: Isolated from the bacterium Herpetosiphon aurantiacus.

References:

1. Nakano, C., Oshima, M., Kurashima, N. and Hoshino, T. Identification of a new diterpene biosynthetic gene cluster that produces O-methylkolavelool in Herpetosiphon aurantiacus. Chembiochem 16 (2015) 772-781. [PMID: 25694050]

[EC 3.1.7.12 created 2017]


EC 3.1.8 Phosphoric Triester Hydrolases

Contents

EC 3.1.8.1 aryldialkylphosphatase
EC 3.1.8.2 diisopropyl-fluorophosphatase


Entries

EC 3.1.8.1

Accepted name: aryldialkylphosphatase

Reaction: An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol

Other name(s): organophosphate hydrolase; paraoxonase; A-esterase; aryltriphosphatase; organophosphate esterase; esterase B1; esterase E4; paraoxon esterase; pirimiphos-methyloxon esterase; OPA anhydrase; organophosphorus hydrolase; phosphotriesterase; paraoxon hydrolase; OPH; organophosphorus acid anhydrase

Systematic name: aryltriphosphate dialkylphosphohydrolase

Comments: Acts on organophosphorus compounds (such as paraoxon) including esters of phosphonic and phosphinic acids. Inhibited by chelating agents; requires divalent cations for activity. Previously regarded as identical with EC 3.1.1.2 arylesterase.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, UM-BBD, CAS registry number: 117698-12-1

References:

1. Aldridge, W.N. Serum esterases. I. Two types of esterase (A and B) hydrolysing p-nitrophenyl acetate, propionate and butyrate and a method for their determination.Biochem. J. 53 (1953) 110-117.

2. Bosmann, H.B. Membrane marker enzymes. Characterization of an arylesterase of guinea pig cerebral cortex utilizing p-nitrophenyl acetate as substrate. Biochim. Biophys. Acta 276 (1972) 180-191. [PMID: 5047702]

3. Mackness, M.I., Thompson, H.M., Hardy, A.R. and Walker, C.H. Distinction between 'A'-esterases and arylesterases. Implications for esterase classification. Biochem. J. 245 (1987) 293-296. [PMID: 2822017]

4. Main, A.R. The differentiation of the A-type esterases in sheep serum. Biochem. J. 75 (1960) 188-195.

5. Reiner, E., Aldridge, W.N. and Hoskin, C.G. (Eds.) Enzymes Hydrolysing Organophosphorus Compounds, Ellis Horwood Ltd., Chichester, UK, 1989.

[EC 3.1.8.1 created 1989]

EC 3.1.8.2

Accepted name: diisopropyl-fluorophosphatase

Reaction: diisopropyl fluorophosphate + H2O = diisopropyl phosphate + fluoride

Other name(s): DFPase; tabunase; somanase; organophosphorus acid anhydrolase; organophosphate acid anhydrase; OPA anhydrase; diisopropylphosphofluoridase; dialkylfluorophosphatase; diisopropyl phosphorofluoridate hydrolase; isopropylphosphorofluoridase; diisopropylfluorophosphonate dehalogenase

Systematic name: diisopropyl-fluorophosphate fluorohydrolase

Comments: Acts on phosphorus anhydride bonds (such as phosphorus-halide and phosphorus-cyanide) in organophosphorus compounds (including 'nerve gases'). Inhibited by chelating agents; requires divalent cations. Related to EC 3.1.8.1 aryldialkylphosphatase. Previously listed as EC 3.8.2.1.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9032-18-2

References:

1. Augustinsson, K.-B. and Heimburger, G. Enzymatic hydrolysis of organophosphorus compounds. I. Occurrence of enzymes hydrolysing dimethyl-amido-ethoxy-phosphoryl cyanide (Tabun). Acta Chem. Scand. 8 (1954) 753-761.

2. Augustinsson, K.-B. and Heimburger, G. Enzymatic hydrolysis of organophosphorus compounds. II. Analysis of reaction products in experiments with Tabun and some properties of blood plasma tabunase. Acta Chem. Scand. 8 (1954) 762-767.

3. Augustinsson, K.-B. and Heimburger, G. Enzymatic hydrolysis of organophosphorus compounds. IV. Specificity studies. Acta Chem. Scand. 8 (1954) 1533-1541.

4. Cohen, J.A. and Warringa, M.G.P.J. Purification and properties of dialkylfluorophosphatase. Biochim. Biophys. Acta 26 (1957) 29-39.

5. Mounter, L.A. Enzymic hydrolysis of organophosphorus compounds. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York, 1960, pp. 541-550.

6. Reiner, E., Aldridge, W.N. and Hoskin, C.G. (Eds.) Enzymes Hydrolysing Organophosphorus Compounds, Ellis Horwood Ltd., Chichester, UK, 1989.

[EC 3.1.8.2 created 1961 as EC 3.8.2.1, transferred 1992 to EC 3.1.8.2]


EC 3.1.11 Exodeoxyribonucleases Producing 5'-Phosphomonoesters

Contents

EC 3.1.11.1 exodeoxyribonuclease I
EC 3.1.11.2 exodeoxyribonuclease III
EC 3.1.11.3 exodeoxyribonuclease (lambda-induced)
EC 3.1.11.4 exodeoxyribonuclease (phage SP3-induced)
EC 3.1.11.5 exodeoxyribonuclease V
EC 3.1.11.6 exodeoxyribonuclease VII

EC 3.1.11.7 adenosine-5'-diphospho-5'-[DNA] diphosphatase
EC 3.1.11.8 guanosine-5'-diphospho-5'-[DNA] diphosphatase


Entries

EC 3.1.11.1

Accepted name: exodeoxyribonuclease I

Reaction: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates

Other name(s): Escherichia coli exonuclease I; E. coli exonuclease I; exonuclease I

Comments: Preference for single-stranded DNA. The Escherichia coli enzyme hydrolyses glucosylated DNA. Formerly EC 3.1.4.25.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9037-46-1

References:

1. Blakesley, R.W., Dodgson, J.B., Nes, I.F. and Wells, R.D. Duplex regions in single-stranded phiX174 DNA are cleaved by a restriction endonuclease from Haemophilus aegyptius. J. Biol. Chem. 252 (1977) 7300-7306. [PMID: 71298]

2. Kelley, R.B., Atkinson, M.R., Huberman, J.A. and Kornberg, A. Excision of thymine dimers and other mismatched sequences by DNA polymerases of Escherichia coli. Nature 224 (1969) 495-501.

3. Lehman, I.R. and Nussbaum, A.L. The deoxyribonucleases of Escherichia coli. V. On the specificity of exonuclease I (phosphodiesterase). J. Biol. Chem. 239 (1964) 2628-2636.

[EC 3.1.11.1 created 1972 as EC 3.1.4.25, transferred 1978 to EC 3.1.11.1]

EC 3.1.11.2

Accepted name: exodeoxyribonuclease III

Reaction: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates

Other name(s): Escherichia coli exonuclease III; E. coli exonuclease III; endoribonuclease III

Comments: Preference for double-stranded DNA. Has endonucleolytic activity near apurinic sites on DNA. Formerly EC 3.1.4.27.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9037-44-9

References:

1. Lindahl, T., Gally, J.A. and Edelman, G.M. Properties of deoxyribonuclease 3 from mammalian tissues. J. Biol. Chem. 244 (1969) 5014-5019. [PMID: 5824576]

2. Richardson, C.C. and Kornberg, A. A deoxyribonucleic acid phosphatase-exonuclease from Escherichia coli. I. Purification of the enzyme and characterization of the phosphatase activity. J. Biol. Chem. 239 (1964) 242-250.

3. Richardson, C.C., Lehman, I.R. and Kornberg, A. A deoxyribonucleic acid phosphatase-exonuclease from Escherichia coli. II. Characterization of the exonuclease activity. J. Biol. Chem. 239 (1964) 251-258.

[EC 3.1.11.2 created 1972 as EC 3.1.4.27, transferred 1978 to EC 3.1.11.2]

EC 3.1.11.3

Accepted name: exodeoxyribonuclease (lambda-induced)

Reaction: Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates

Other name(s): lambda exonuclease; phage lambda-induced exonuclease; Escherichia coli exonuclease IV; E. coli exonuclease IV; exodeoxyribonuclease IV; exonuclease IV

Comments: Preference for double-stranded DNA. Does not attack single-strand breaks. Formerly EC 3.1.4.28.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37367-70-7

References:

1. Lindahl, T., Gally, J.A. and Edelman, G.M. Deoxyribonuclease IV: a new exonuclease from mammalian tissues. Proc. Natl. Acad. Sci. USA 62 (1969) 597-603. [PMID: 5256235]

2. Little, J.W. An exonuclease induced by bacteriophage lambda. II. Nature of the enzymatic reaction. J. Biol. Chem. 242 (1967) 679-686. [PMID: 6017737]

[EC 3.1.11.3 created 1972 as EC 3.1.4.28, transferred 1978 to EC 3.1.11.3]

EC 3.1.11.4

Accepted name: exodeoxyribonuclease (phage SP3-induced)

Reaction: Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates

Other name(s): phage SP3 DNase; DNA 5'-dinucleotidohydrolase; deoxyribonucleate 5'-dinucleotidase; deoxyribonucleic 5'-dinucleotidohydrolase; bacteriophage SP3 deoxyribonuclease; deoxyribonucleate 5'-dinucleotidase

Comments: Preference for single-stranded DNA. Formerly EC 3.1.4.31.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37288-30-5

References:

1. Trilling, D.M. and Aposhian, H.V. Sequential cleavage of dinucleotides from DNA by phage Sp3 DNAse. Proc. Natl. Acad. Sci. USA 60 (1968) 214-221. [PMID: 4968633]

[EC 3.1.11.4 created 1972 as EC 3.1.4.31, transferred 1978 to EC 3.1.11.4]

EC 3.1.11.5

Accepted name: exodeoxyribonuclease V

Reaction: Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides

Other name(s): Escherichia coli exonuclease V; E. coli exonuclease V; gene recBC endoenzyme; RecBC deoxyribonuclease; gene recBC DNase; exonuclease V; gene recBCD enzymes

Comments: Preference for double-stranded DNA. Possesses DNA-dependent ATPase activity. Acts endonucleolytically on single-stranded circular DNA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37350-26-8

References:

1. Eichler, D.C. and Lehman, I.R. On the role of ATP in phosphodiester bond hydrolysis catalyzed by the recBC deoxyribonuclease of Escherichia coli. J. Biol. Chem. 252 (1977) 499-503. [PMID: 319095]

2. Goldmark, P.J. and Liun, S. Purification and properties of the recBC DNase of Escherichia coli K-12. J. Biol. Chem. 247 (1972) 1849-1860. [PMID: 4552016]

3. Oishi, M. An ATP-dependent deoxyribonuclease from Escherichia coli with a possible role in genetic recombination. Proc. Natl. Acad. Sci. USA 64 (1969) 1292-1299. [PMID: 4916924]

4. Wright, M., Buttin, G. and Hurwitz, J. The isolation and characterization from Escherichia coli of an adenosine triphosphate-dependent deoxyribonuclease directed by rec B, C genes. J. Biol. Chem. 246 (1971) 6543-6555. [PMID: 4332130]

[EC 3.1.11.5 created 1978]

EC 3.1.11.6

Accepted name: exodeoxyribonuclease VII

Reaction: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates

Other name(s): Escherichia coli exonuclease VII; E. coli exonuclease VII; endodeoxyribonuclease VII; exonuclease VII

Comments: Preference for single-stranded DNA.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 52933-20-7

References:

1. Chase, J.W. and Richardson, C.C. Ribonuclease VII of Escherichia coli. J. Biol. Chem. 249 (1974) 4545-4552.

2. Chase, J.W. and Richardson, C.C. Exonuclease VII of Escherichia coli. J. Biol. Chem. 249 (1974) 4553-4561.

[EC 3.1.11.6 created 1978]

EC 3.1.11.7

Accepted name: adenosine-5'-diphospho-5'-[DNA] diphosphatase

Reaction: (1) adenosine-5'-diphospho-5'-[DNA] + H2O = AMP + phospho-5'-[DNA]
(2) adenosine-5'-diphospho-5'-(ribonucleotide)-[DNA] + H2O = AMP + 5'-phospho-(ribonucleotide)-[DNA]

Other name(s): aprataxin; 5'-App5'-DNA adenylate hydrolase; APTX (gene name); HNT3 (gene name)

Systematic name: adenosine-5'-diphospho-5'-[DNA] hydrolase (adenosine 5'-phosphate-forming)

Comments: Aprataxin is a DNA-binding protein involved in different types of DNA break repair. The enzyme acts (among other activities) on abortive DNA ligation intermediates that contain an adenylate covalently linked to the 5'-phosphate DNA terminus. It also acts when the adenylate is covalently linked to the 5'-phosphate of a ribonucleotide linked to a DNA strand, which is the result of abortive ligase activty on products of ../26/4.html, ribonuclease H, an enzyme that cleaves RNA-DNA hybrids on the 5' side of the ribonucleotide found in the 5'-RNA-DNA-3' junction. Aprataxin binds the adenylate group to a histidine residue within the active site, followed by its hydrolysis from the nucleic acid and eventual release, leaving a 5'-phosphate terminus that can be efficiently rejoined. The enzyme also possesses the activities of EC 3.1.11.8, guanosine-5'-diphospho-5'-[DNA] diphosphatase, and EC 3.1.12.2, DNA-3'-diphospho-5'-guanosine diphosphatase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Ahel, I., Rass, U., El-Khamisy, S.F., Katyal, S., Clements, P.M., McKinnon, P.J., Caldecott, K.W. and West, S.C. The neurodegenerative disease protein aprataxin resolves abortive DNA ligation intermediates. Nature 443 (2006) 713-716. [PMID: 16964241]

2. Tumbale, P., Williams, J.S., Schellenberg, M.J., Kunkel, T.A. and Williams, R.S. Aprataxin resolves adenylated RNA-DNA junctions to maintain genome integrity. Nature 506 (2014) 111-115. [PMID: 24362567]

[EC 3.1.11.7 created 2017]

EC 3.1.11.8

Accepted name: guanosine-5'-diphospho-5'-[DNA] diphosphatase

Reaction: guanosine-5'-diphospho-5'-[DNA] + H2O = phospho-5'-[DNA] + GMP

Other name(s): aprataxin; pp5'G5'DNA diphosphatase; pp5'G5'-DNA guanylate hydrolase; APTX (gene name); HNT3 (gene name)

Systematic name: guanosine-5'-diphospho-5'-[DNA] hydrolase (guanosine 5'-phosphate-forming)

Comments: Aprataxin is a DNA-binding protein that catalyses (among other activities) the 5' decapping of Gpp-DNA (formed by homologs of RtcB3 from the bacterium Myxococcus xanthus).The enzyme binds the guanylate group to a histidine residue at its active site, forming a covalent enzyme-nucleotide phosphate intermediate, followed by the hydrolysis of the guanylate from the nucleic acid and eventual release. The enzyme forms a 5'-phospho terminus that can be efficiently joined by "classical" ligases. The enzyme also possesses the activitiy of EC 3.1.11.7, adenosine-5'-diphospho-5'-[DNA] diphosphatase and EC 3.1.12.2, DNA-3'-diphospho-5'-guanosine diphosphatase.

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Maughan, W.P. and Shuman, S. Characterization of 3'-phosphate RNA ligase paralogs RtcB1, RtcB2, and RtcB3 from Myxococcus xanthus highlights DNA and RNA 5'-phosphate capping activity of RtcB3. J. Bacteriol. 197 (2015) 3616-3624. [PMID: 26350128]

[EC 3.1.11.8 created 2017]


EC 3.1.12 Exodeoxyribonucleases Producing 3'-Phosphomonoesters

Contents

EC 3.1.12.1 5' to 3' exodeoxyribonuclease (nucleoside 3'-phosphate-forming)
EC 3.1.12.2 DNA-3'-diphospho-5'-guanosine diphosphatase

EC 3.1.12.1

Accepted name: 5' to 3' exodeoxyribonuclease (nucleoside 3'-phosphate-forming)

Reaction: exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates

Other name(s): Cas4; 5' to 3' single stranded DNA exonuclease

Comments: Preference for single-stranded DNA. The enzyme from the archaeon Sulfolobus solfataricus contains a [4Fe-4S] cluster and requires a divalent metal cation, such as Mg2+ or Mn2+, for activity.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Zhang, J., Kasciukovic, T. and White, M.F. The CRISPR associated protein Cas4 Is a 5' to 3' DNA exonuclease with an iron-sulfur cluster. PLoS One 7 (2012) e47232. [PMID: 23056615]

2. Lemak, S., Beloglazova, N., Nocek, B., Skarina, T., Flick, R., Brown, G., Popovic, A., Joachimiak, A., Savchenko, A. and Yakunin, A.F. Toroidal structure and DNA cleavage by the CRISPR-associated [4Fe-4S]-cluster containing Cas4 nuclease SSO0001 from Sulfolobus solfataricus. J. Am. Chem. Soc. 135 (2013) 17476-17487. [PMID: 24171432]

[EC 3.1.12.1 created 2014]

EC 3.1.12.2

Accepted name: DNA-3'-diphospho-5'-guanosine diphosphatase

Reaction: [DNA]-3'-diphospho-5'-guanosine + H2O = [DNA]-3'-phosphate + GMP

Other name(s): aprataxin; DNA-3'pp5'G guanylate hydrolase; APTX (gene name); HNT3 (gene name)

Systematic name: [DNA]-3'-diphospho-5'-guanosine hydrolase (guanosine 5'-phosphate-forming)

Comments: Aprataxin is a DNA-binding protein that catalyses (among other activities) the 3' decapping of DNA-ppG (formed by EC 6.5.1.8, 3'-phosphate/5'-hydroxy nucleic acid ligase) [1]. The enzyme binds the guanylate group to a histidine residue at its active site, forming a covalent enzyme-nucleotide phosphate intermediate, followed by the hydrolysis of the guanylate from the nucleic acid and its eventual release. The enzyme also possesses the activity of EC 3.1.11.7, adenosine-5'-diphospho-5'-[DNA] diphosphatase, and EC 3.1.11.8, guanosine-5'-diphospho-5'-[DNA] diphosphatase.

BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:

References:

1. Das, U., Chauleau, M., Ordonez, H. and Shuman, S. Impact of DNA3'pp5'G capping on repair reactions at DNA 3' ends. Proc. Natl. Acad. Sci. USA 111 (2014) 11317-11322. [PMID: 25049385]

2. Chauleau, M., Jacewicz, A. and Shuman, S. DNA3'pp5'G de-capping activity of aprataxin: effect of cap nucleoside analogs and structural basis for guanosine recognition. Nucleic Acids Res. 43 (2015) 6075-6083. [PMID: 26007660]

[EC 3.1.12.2 created 2017]


EC 3.1.13 Exoribonucleases Producing 5'-Phosphomonoesters

Contents

EC 3.1.13.1 exoribonuclease II
EC 3.1.13.2 exoribonuclease H
EC 3.1.13.3 oligonucleotidase
EC 3.1.13.4 poly(A)-specific ribonuclease
EC 3.1.13.5 ribonuclease D


Entries

EC 3.1.13.1

Accepted name: exoribonuclease II

Reaction: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates

Other name(s): ribonuclease II; ribonuclease Q; BN ribonuclease; Escherichia coli exo-RNase II; RNase II; exoribonuclease; 5'-exoribonuclease

Comments: Preference for single-stranded RNA. The enzyme processes 3'-terminal extra-nucleotides of monomeric tRNA precursors, following the action of EC 3.1.26.5 ribonuclease P. Formerly EC 3.1.4.20.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37288-24-7

References:

1. Nossal, N.G. and Singer, M. The processive degradation of individual polyribonucleotide chains. I. Escherichia coli ribonuclease II. J. Biol. Chem. 243 (1968) 913-922. [PMID: 4867942]

2. Schmidt, F.J. and McClain, W.H. An Escherichia coli ribonuclease which removes an extra nucleotide from a biosynthetic intermediate of bacteriophage T4 proline transfer RNA. Nucleic Acids Res. 5 (1978) 4129-4139. [PMID: 364422]

3. Shimura, Y., Sakano, H. and Nagawa, F. Specific ribonucleases involved in processing of tRNA precursors of Escherichia coli. Partial purification and some properties. Eur. J. Biochem. 86 (1978) 267-281. [PMID: 350582]

4. Sporn, M.B., Lazarus, H.M. Smith, J.M. and Henderson, W.R. Studies on nuclear exoribonucleases. 3. Isolation and properties of the enzyme from normal and malignant tissues of the mouse. Biochemistry 8 (1969) 1698-1706. [PMID: 5805304]

[EC 3.1.13.1 created 1972 as EC 3.1.4.20, transferred 1978 to EC 3.1.13.1]

EC 3.1.13.2

Accepted name: exoribonuclease H

Reaction: 3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid

Comments: This is a secondary reaction to the RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end performed by EC 3.1.26.13 (retroviral ribonuclease H).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Schatz, O., Mous, J. and Le Grice, S.F. HIV-1 RT-associated ribonuclease H displays both endonuclease and 3'—5' exonuclease activity. EMBO J. 9 (1990) 1171-1176. [PMID: 1691093]

[EC 3.1.13.2 created 1978, modified 2010]

EC 3.1.13.3

Accepted name: oligonucleotidase

Reaction: Exonucleolytic cleavage of oligonucleotides to yield nucleoside 5'-phosphates

Other name(s): oligoribonuclease

Comments: Also hydrolyses NAD+ to NMN and AMP. Formerly EC 3.1.4.19.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37288-23-6

References:

1. Futai, M. and Mizuno, D. A new phosphodiesterase forming nucleoside 5'-monophosphate from rat liver. Its partial purification and substrate specificity for nicotinamide adenine dinucleotide and oligonucleotides. J. Biol. Chem. 242 (1967) 5301-5307. [PMID: 4294333]

[EC 3.1.13.3 created 1972 as EC 3.1.4.19, transferred 1978 to EC 3.1.13.3]

EC 3.1.13.4

Accepted name: poly(A)-specific ribonuclease

Reaction: Exonucleolytic cleavage of poly(A) to 5'-AMP

Other name(s): 3'-exoribonuclease; 2',3'-exoribonuclease

Comments: Cleaves poly(A) in either the single- or double-stranded form.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 110541-21-4

References:

1. Schröder, H.C., Zahn, R.K., Dose, K. and Müller, E.G. Purification and characterization of a poly(A)-specific exoribonuclease from calf thymus. J. Biol. Chem. 255 (1980) 4535-4538. [PMID: 6246077]

[EC 3.1.13.4 created 1984]

EC 3.1.13.5

Accepted name: ribonuclease D

Reaction: Exonucleolytic cleavage that removes extra residues from the 3'-terminus of tRNA to produce 5'-mononucleotides

Other name(s): RNase D

Comments: Requires divalent cations for activity (Mg2+, Mn2+ or Co2+). Alteration of the 3'-terminal base has no effect on the rate of hydrolysis whereas modification of the 3'-terminal sugar has a major effect. tRNA terminating with a 3'-phosphate is completely inactive [3]. This enzyme can convert a tRNA precursor into a mature tRNA [2].

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:

References:

1. Ghosh, R.K. and Deutscher, M.P. Identification of an Escherichia coli nuclease acting on structurally altered transfer RNA molecules. J. Biol. Chem. 253 (1978) 997-1000. [PMID: 342522]

2. Cudny, H., Zaniewski, R. and Deutscher, M.P. Escherichia coli RNase D. Purification and structural characterization of a putative processing nuclease. J. Biol. Chem. 256 (1981) 5627-5632. [PMID: 6263885]

3. Cudny, H., Zaniewski, R. and Deutscher, M.P. Escherichia coli RNase D. Catalytic properties and substrate specificity. J. Biol. Chem. 256 (1981) 5633-5637. [PMID: 6263886]

4. Zhang, J.R. and Deutscher, M.P. Cloning, characterization, and effects of overexpression of the Escherichia coli rnd gene encoding RNase D. J. Bacteriol. 170 (1988) 522-527. [PMID: 2828310]

[EC 3.1.13.5 created 2006]


EC 3.1.14 Exoribonucleases Producing 3'-Phosphomonoesters

EC 3.1.14.1

Accepted name: yeast ribonuclease

Reaction: Exonucleolytic cleavage to nucleoside 3'-phosphates

Comments: Similar enzyme: RNase U4.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:

References:

1. Otaka, Y., Uchida, T. and Sakai, T. Purification and properties of ribonuclease from yeast. J. Biochem (Tokyo) 54 (1963) 322-327.

[EC 3.1.14.1 created 1978]


EC 3.1.15 Exonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 5'-Phosphomonoesters

EC 3.1.15.1

Accepted name: venom exonuclease

Reaction: Exonucleolytic cleavage in the 3'- to 5'- direction to yield nucleoside 5'-phosphates

Other name(s): venom phosphodiesterase

Comments: Preference for single-stranded substrate.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9025-82-5

References:

1. Laskowski, M., Sr. Pancreatic deoxyribonuclease I, in Cantoni, G.L. and Davies, D.R. (Eds.), Procedures in Nucleic Acid Research, Harper and Row, New York, 1966, pp. 85-101.

[EC 3.1.15.1 created 1978]


EC 3.1.16 Exonucleases Active with either Ribo- or Deoxyribonucleic Acids and Producing 3'-Phosphomonoesters

EC 3.1.16.1

Accepted name: spleen exonuclease

Reaction: Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates

Other name(s): 3'-exonuclease; spleen phosphodiesterase; 3'-nucleotide phosphodiesterase; phosphodiesterase II

Comments: Preference for single-stranded substrate. Formerly EC 3.1.4.18 (cf. EC 3.1.31.1 micrococcal nuclease).

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9068-54-6

References:

1. Bernardi, A. and Bernardi, G. Spleen acid nuclease, in Boyer, P.D. (Ed.), The Enzymes, 3rd edn., vol. 4, Academic Press, New York, 1971, pp. 329-336.

[EC 3.1.16.1 created 1972 as EC 3.1.4.18, transferred 1978 to EC 3.1.16.1]


Continued with EC 3.1.21.1 to EC 3.1.31.1
Return to EC 3 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page