Continued from EC 3.1.4.1 to EC 3.1.4.51
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
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.
Accepted name: arylsulfatase (type I)
Reaction: an aryl sulfate + H2O = a phenol + sulfate
Other name(s): sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; type I sulfatase; arylsulfatase
Systematic name: aryl-sulfate sulfohydrolase
Comments: Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-β-lactamase fold and binds two zinc ions as cofactors. Arylsulfatases are type I enzymes, found in both prokaryotes and eukaryotes, with rather similar specificities. The key catalytic residue 3-oxo-L-alanine initiates the reaction through a nucleophilic attack on the sulfur atom in the substrate. This residue is generated by posttranslational modification of a conserved cysteine or serine residue by EC 1.8.3.7, formylglycine-generating enzyme, EC 1.1.98.7, serine-type anaerobic sulfatase-maturating enzyme, or EC 1.8.98.7, cysteine-type anaerobic sulfatase-maturating enzyme.
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. [PMID: 13363831]
2. 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. [PMID: 13843260]
3. Roy, A.B. The synthesis and hydrolysis of sulfate esters. Adv. Enzymol. Relat. Subj. Biochem. 22 (1960) 205-235. [PMID: 13744184]
4. Roy, A.B. Sulphatases, lysosomes and disease. Aust. J. Exp. Biol. Med. Sci. 54 (1976) 111-135. [PMID: 13772]
5. Schmidt, B., Selmer, T., Ingendoh, A. and von Figura, K. A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell 82 (1995) 271-278. [PMID: 7628016]
6. Dierks, T., Miech, C., Hummerjohann, J., Schmidt, B., Kertesz, M.A. and von Figura, K. Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine. J. Biol. Chem. 273 (1998) 25560-25564. [PMID: 9748219]
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.
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.
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 3.1.6.5 Deleted entry: sinigrin sulfohydrolase; myrosulfatase (EC 3.1.6.5 created 1961, deleted 1964)]
Accepted name: choline-sulfatase
Reaction: choline sulfate + H2O = choline + sulfate
Systematic name: choline-sulfate sulfohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, 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.
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.
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]
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]
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]
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]
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]
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, PDB, CAS registry number: 50936-59-9
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]
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, PDB, 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]
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]
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]
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]
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, PDB, 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]
Accepted name: (R)-specific secondary-alkylsulfatase (type III)
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; (R)-specific secondary-alkylsulfatase
Systematic name: (R)-secondary-alkyl sulfate sulfohydrolase [(S)-secondary-alcohol forming]
Comments: Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-β-lactamase fold and binds two zinc ions as cofactors. This enzyme belongs to the type III sulfatase family. The enzyme from the bacterium Rhodococcus ruber prefers linear secondary-alkyl sulfate esters, particularly octan-2-yl, octan-3-yl, and octan-4-yl sulfates [1]. The enzyme from the bacterium Pseudomonas sp. DSM6611 utilizes a range of secondary-alkyl sulfate esters bearing aromatic, olefinic and acetylenic moieties. Hydrolysis proceeds through inversion of the configuration at the stereogenic carbon atom, resulting in perfect enantioselectivity. cf. EC 3.1.6.1, arylsulfatase (type I), and EC 1.14.11.77, alkyl sulfatase (type II).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, 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.
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]
Accepted name: linear primary-alkylsulfatase
Reaction: a primary alkyl sulfate ester + H2O = an alcohol + sulfate
Other name(s): sdsA1 (gene name); yjcS (gene name); type III linear primary-alkylsulfatase
Systematic name: primary alkyl sulfate ester sulfohydrolase
Comments: Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-β-lactamase fold and binds two zinc ions as cofactors. This enzyme belongs to the type III sulfatase family. The enzyme is active against linear primary-alkyl sulfate esters, such as dodecyl sulfate, decyl sulfate, octyl sulfate, and hexyl sulfate. It The enzyme from Pseudomonas aeruginosa is secreted out of the cell. The catalytic mechanism begins with activation of a water molecule by the binuclear Zn2+ cluster, resulting in a nucleophilic attack on the carbon atom. cf. EC 3.1.6.22, branched primary-alkylsulfatase, and EC 3.1.6.19, (R)-specific secondary-alkylsulfatase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Hagelueken, G., Adams, T.M., Wiehlmann, L., Widow, U., Kolmar, H., Tummler, B., Heinz, D.W. and Schubert, W.D. The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas aeruginosa, defines a third class of sulfatases. Proc. Natl. Acad. Sci. USA 103 (2006) 7631-7636. [PMID: 16684886]
2. Long, M., Ruan, L., Li, F., Yu, Z. and Xu, X. Heterologous expression and characterization of a recombinant thermostable alkylsulfatase (sdsAP). Extremophiles 15 (2011) 293-301. [PMID: 21318560]
3. Liang, Y., Gao, Z., Dong, Y. and Liu, Q. Structural and functional analysis show that the Escherichia coli uncharacterized protein YjcS is likely an alkylsulfatase. Protein Sci. 23 (2014) 1442-1450. [PMID: 25066955]
4. Sun, L., Chen, P., Su, Y., Cai, Z., Ruan, L., Xu, X. and Wu, Y. Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9. Biosci Rep 37 (2017) . [PMID: 28442601]
Accepted name: branched primary-alkylsulfatase
Reaction: 2-butyloctyl sulfate + H2O = 2-butyloctan-1-ol + sulfate
Other name(s): DP1 (gene name); type III branched primary-alkylsulfatase
Systematic name: branched primary-alkyl sulfate ester sulfohydrolase
Comments: Sulfatase enzymes are classified as type I, in which the key catalytic residue is 3-oxo-L-alanine, type II, which are non-heme iron-dependent dioxygenases, or type III, whose catalytic domain adopts a metallo-β-lactamase fold and binds two zinc ions as cofactors. This enzyme belongs to the type III family. The enzyme, characterized from a Pseudomonas strain, is specific for branched primary-alkyl sulfate esters and does not act on linear substrates such as dodecyl sulfate. cf. EC 3.1.6.1, arylsulfatase (type I), EC 1.14.11.77, alkyl sulfatase, EC 3.1.6.19, (R)-specific secondary-alkylsulfatase (type III) and EC 3.1.6.21, linear primary-alkylsulfatase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Ellis, A.J., Hales, S.G., Ur-Rehman, N.G. and White, G.F. Novel alkylsulfatases required for biodegradation of the branched primary alkyl sulfate surfactant 2-butyloctyl sulfate. Appl. Environ. Microbiol. 68 (2002) 31-36. [PMID: 11772605]
2. Toesch, M., Schober, M. and Faber, K. Microbial alkyl- and aryl-sulfatases: mechanism, occurrence, screening and stereoselectivities. Appl. Microbiol. Biotechnol. 98 (2014) 1485-1496. [PMID: 24352732]
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]
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]
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 3.1.7.4 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)]
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]
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, PDB, 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 3.1.7.7 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 Transferred entry: tuberculosinol synthase. Now known to be partial activity of EC 2.5.1.153, adenosine tuberculosinyltransferase. (EC 3.1.7.8 created 2011, deleted 2020)]
[EC 3.1.7.9 Transferred entry: isotuberculosinol synthase. Now known to be partial activity of EC 2.5.1.153, adenosine tuberculosinyltransferase. (EC 3.1.7.9 created 2011, deleted 2020)]
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]
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]
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]
Accepted name: neryl diphosphate diphosphatase
Reaction: neryl diphosphate + H2O = nerol + diphosphate
For diagram of reaction, click here
Glossary: nerol = (2Z)-3,7-dimethylocta-2,6-dien-1-ol
Other name(s): NES (gene name); nerol synthase
Systematic name: neryl-diphosphate diphosphohydrolase
Comments: The enzyme, characterized from Glycine max (soybeans), is specific for neryl diphosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Zhang, M., Liu, J., Li, K. and Yu, D. Identification and characterization of a novel monoterpene synthase from soybean restricted to neryl diphosphate precursor. PLoS One 8 (2013) e75972. [PMID: 24124526]
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 (ambiguous); 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, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, 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 3.1.8.2 Transferred entry: diisopropyl-fluorophosphatase. Now classified as EC 3.8.2.2, diisopropyl-fluorophosphatase (EC 3.1.8.2 created 1961 as EC 3.8.2.1, transferred 1992 to EC 3.1.8.2, deleted 2023)]
EC 3.1.11.7 transferred, now EC 3.6.1.71
EC 3.1.11.8 transferred, now EC 3.6.1.70
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.
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.
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]
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]
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]
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 3.1.11.7 Transferred entry: adenosine-5'-diphospho-5'-[DNA] diphosphatase, Now EC 3.6.1.71, adenosine-5'-diphospho-5'-[DNA] diphosphatase (EC 3.1.11.7 created 2017, deleted 2019)]
[EC 3.1.11.8 Transferred entry: guanosine-5'-diphospho-5'-[DNA] diphosphatase. Now EC 3.6.1.70, guanosine-5'-diphospho-5'-[DNA] diphosphatase (EC 3.1.11.8 created 2017, deleted 2019)]
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, PDB, 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 3.1.12.2 Transferred entry: DNA-3-diphospho-5-guanosine diphosphatase. Now EC 3.6.1.72, DNA-3-diphospho-5-guanosine diphosphatase (EC 3.1.12.2 created 2017, deleted 2019)]
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]
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]
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, PDB, 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]
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]
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]
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.
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.
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, PDB, 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.