Continued from EC 3.2.1.151 to 3.2.1.226
EC 3.2.2 Hydrolysing N-Glycosyl Compounds
EC 3.2.3 Hydrolysing S-Glycosyl Compounds
Accepted name: purine nucleosidase
Reaction: a purine nucleoside + H2O = D-ribose + a purine base
Other name(s): nucleosidase (misleading); purine β-ribosidase; purine nucleoside hydrolase; purine ribonucleosidase; ribonucleoside hydrolase (misleading); nucleoside hydrolase (misleading); N-ribosyl purine ribohydrolase; nucleosidase g; N-D-ribosylpurine ribohydrolase; inosine-adenosine-guanosine preferring nucleoside hydrolase; purine-specific nucleoside N-ribohydrolase; IAG-nucleoside hydrolase; IAG-NH
Systematic name: purine-nucleoside ribohydrolase
Comments: The enzyme from the bacterium Ochrobactrum anthropi specifically catalyses the irreversible N-riboside hydrolysis of purine nucleosides. Pyrimidine nucleosides, purine and pyrimidine nucleotides, NAD+, NADP+ and nicotinaminde mononucleotide are not substrates [6].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-44-9
References:
1. Heppel, L.A. and Hilmoe, R.J. Phosphorolysis and hydrolysis of purine ribosides from yeast. J. Biol. Chem. 198 (1952) 683-694. [PMID: 12999785]
2. Kalckar, H.M. Biosynthetic aspects of nucleosides and nucleic acids. Pubbl. Staz. Zool. (Napoli) 23 (1951) 87-103.
3. Takagi, Y. and Horecker, B.L. Purification and properties of a bacterial riboside hydrolyase. J. Biol. Chem. 225 (1956) 77-86. [PMID: 13416219]
4. Tarr, H.L.A. Fish muscle riboside hydrolases. Biochem. J. 59 (1955) 386-391. [PMID: 14363106]
5. Parkin, D.W. Purine-specific nucleoside N-ribohydrolase from Trypanosoma brucei brucei. Purification, specificity, and kinetic mechanism. J. Biol. Chem. 271 (1996) 21713-21719. [PMID: 8702965]
6. Ogawa, J., Takeda, S., Xie, S.X., Hatanaka, H., Ashikari, T., Amachi, T. and Shimizu, S. Purification, characterization, and gene cloning of purine nucleosidase from Ochrobactrum anthropi. Appl. Environ. Microbiol. 67 (2001) 1783-1787. [PMID: 11282633]
7. Versées, W., Decanniere, K., Van Holsbeke, E., Devroede, N. and Steyaert, J. Enzyme-substrate interactions in the purine-specific nucleoside hydrolase from Trypanosoma vivax. J. Biol. Chem. 277 (2002) 15938-15946. [PMID: 11854281]
8. Mazumder-Shivakumar, D. and Bruice, T.C. Computational study of IAG-nucleoside hydrolase: determination of the preferred ground state conformation and the role of active site residues. Biochemistry 44 (2005) 7805-7817. [PMID: 15909995]
Accepted name: inosine nucleosidase
Reaction: inosine + H2O = D-ribose + hypoxanthine
Other name(s): inosinase; inosine-guanosine nucleosidase
Systematic name: inosine ribohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9030-95-9
References:
1. Koch, A.L. Some enzymes of nucleoside metabolism of Escherichia coli. J. Biol. Chem. 223 (1956) 535-549.
2. Tarr, H.L.A. Fish muscle riboside hydrolases. Biochem. J. 59 (1955) 386-391.
Accepted name: uridine nucleosidase
Reaction: uridine + H2O = D-ribose + uracil
Other name(s): uridine hydrolase
Systematic name: uridine ribohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9025-47-2
References:
1. Carter, C.E. Partial purification of a non-phosphorylytic uridine nucleosidase from yeast. J. Am. Chem. Soc. 73 (1951) 1508-1510.
Accepted name: AMP nucleosidase
Reaction: AMP + H2O = D-ribose 5-phosphate + adenine
Other name(s): adenylate nucleosidase; adenosine monophosphate nucleosidase
Systematic name: AMP phosphoribohydrolase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9025-45-0
References:
1. Hurwitz, J., Heppel, L.A. and Horecker, B.L. The enzymatic cleavage of adenylic acid to adenine and ribose 5-phosphate. J. Biol. Chem. 226 (1957) 525-540.
Accepted name: NAD+ glycohydrolase
Reaction: NAD+ + H2O = ADP-D-ribose + nicotinamide
Glossary: ADP-D-ribose = adenosine 5′-(5-deoxy-D-ribofuranos-5-yl diphosphate)
Other name(s): NAD glycohydrolase; nicotinamide adenine dinucleotide glycohydrolase; β-NAD+ glycohydrolase; DPNase (ambiguous); NAD hydrolase (ambiguous); diphosphopyridine nucleosidase (ambiguous); nicotinamide adenine dinucleotide nucleosidase (ambiguous); NAD nucleosidase (ambiguous); DPN hydrolase (ambiguous); NADase (ambiguous); nga (gene name)
Systematic name: NAD+ glycohydrolase
Comments: This enzyme catalyses the hydrolysis of NAD+, without associated ADP-ribosyl cyclase activities (unlike the metazoan enzyme EC 3.2.2.6, bifunctional ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase). The enzyme from Group A streptococci has been implicated in the pathogenesis of diseases such as streptococcal toxic shock-like syndrome (STSS) and necrotizing fasciitis. The enzyme from the venom of the snake Agkistrodon acutus also catalyses EC 3.6.1.5, apyrase [3].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9025-46-1
References:
1. Fehrenbach, F.J. Reinigung und Kristallisation der NAD-Glykohydrolase aus C-Streptokokken. Eur. J. Biochem. 18 (1971) 94-102. [PMID: 4322210]
2. Grushoff, P.S., Shany, S. and Bernheimer, A.W. Purification and properties of streptococcal nicotinamide adenine dinucleotide glycohydrolase. J. Bacteriol. 122 (1975) 599-605. [PMID: 236282]
3. Zhang, L., Xu, X., Luo, Z., Shen, D. and Wu, H. Identification of an unusual AT(D)Pase-like activity in multifunctional NAD glycohydrolase from the venom of Agkistrodon acutus. Biochimie 91 (2009) 240-251. [PMID: 18952139]
4. Ghosh, J., Anderson, P.J., Chandrasekaran, S. and Caparon, M.G. Characterization of Streptococcus pyogenes β-NAD+ glycohydrolase: re-evaluation of enzymatic properties associated with pathogenesis. J. Biol. Chem. 285 (2010) 5683-5694. [PMID: 20018886]
5. Smith, C.L., Ghosh, J., Elam, J.S., Pinkner, J.S., Hultgren, S.J., Caparon, M.G. and Ellenberger, T. Structural basis of Streptococcus pyogenes immunity to its NAD+ glycohydrolase toxin. Structure 19 (2011) 192-202. [PMID: 21300288]
Accepted name: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Reaction: NAD+ + H2O = ADP-D-ribose + nicotinamide (overall reaction)
(1a) NAD+ = cyclic ADP-ribose + nicotinamide
(1b) cyclic ADP-ribose + H2O = ADP-D-ribose
For diagram of reaction click here.
Glossary: ADP-D-ribose = adenosine 5'-(5-deoxy-D-ribofuranos-5-yl diphosphate)
cyclic ADP-ribose = N1-(β-D-ribosyl)adenosine 5'(P1),5''(P2)-cyclic diphosphate
Other name(s): NAD+ nucleosidase; NADase (ambiguous); DPNase (ambiguous); DPN hydrolase (ambiguous); NAD hydrolase (ambiguous); nicotinamide adenine dinucleotide nucleosidase (ambiguous); NAD glycohydrolase (misleading); NAD nucleosidase (ambiguous); nicotinamide adenine dinucleotide glycohydrolase (misleading); CD38 (gene name); BST1 (gene name)
Systematic name: NAD+ glycohydrolase (cyclic ADP-ribose-forming)
Comments: This multiunctional enzyme catalyses both the synthesis and hydrolysis of cyclic ADP-ribose, a calcium messenger that can mobilize intracellular Ca2+ stores and activate Ca2+ influx to regulate a wide range of physiological processes. In addition, the enzyme also catalyses EC 2.4.99.20, 2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase. It is also able to act on β-nicotinamide D-ribonucleotide. cf. EC 3.2.2.5, NAD+ glycohydrolase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9032-65-9
References:
1. Imai, T. Purification and characterization of a pyridine nucleotide glycohydrolase from rabbit spleen. J. Biochem. 106 (1989) 928Ð937. [PMID: 2613697]
2. Howard, M., Grimaldi, J.C., Bazan, J.F., Lund, F.E., Santos-Argumedo, L., Parkhouse, R.M., Walseth, T.F. and Lee, H.C. Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38. Science 262 (1993) 1056-1059. [PMID: 8235624]
3. Takasawa, S., Tohgo, A., Noguchi, N., Koguma, T., Nata, K., Sugimoto, T., Yonekura, H. and Okamoto, H. Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP. J. Biol. Chem. 268 (1993) 26052-26054. [PMID: 8253715]
4. Tohgo, A., Takasawa, S., Noguchi, N., Koguma, T., Nata, K., Sugimoto, T., Furuya, Y., Yonekura, H. and Okamoto, H. Essential cysteine residues for cyclic ADP-ribose synthesis and hydrolysis by CD38. J. Biol. Chem. 269 (1994) 28555-28557. [PMID: 7961800]
5. Fryxell, K.B., O'Donoghue, K., Graeff, R.M., Lee, H.C. and Branton, W.D. Functional expression of soluble forms of human CD38 in Escherichia coli and Pichia pastoris. Protein Expr. Purif. 6 (1995) 329-336. [PMID: 7663169]
6. Yamamoto-Katayama, S., Ariyoshi, M., Ishihara, K., Hirano, T., Jingami, H. and Morikawa, K. Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities. J. Mol. Biol. 316 (2002) 711-723. [PMID: 11866528]
7. Liu, Q., Kriksunov, I.A., Graeff, R., Munshi, C., Lee, H.C. and Hao, Q. Crystal structure of human CD38 extracellular domain. Structure 13 (2005) 1331-1339. [PMID: 16154090]
Accepted name: adenosine nucleosidase
Reaction: adenosine + H2O = D-ribose + adenine
Other name(s): adenosinase; N-ribosyladenine ribohydrolase; adenosine hydrolase; ANase
Systematic name: adenosine ribohydrolase
Comments: Also acts on adenosine N-oxide.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 9075-41-6
References:
1. Mazelis, M. and Creveling, R.K. An adenosine hydrolase from brussels sprouts. J. Biol. Chem. 238 (1963) 3358-3361.
Accepted name: ribosylpyrimidine nucleosidase
Reaction: a pyrimidine nucleoside + H2O = D-ribose + a pyrimidine base
Other name(s): N-ribosylpyrimidine nucleosidase; pyrimidine nucleosidase; N-ribosylpyrimidine ribohydrolase; pyrimidine nucleoside hydrolase; RihB; YeiK; nucleoside ribohydrolase
Systematic name: pyrimidine-nucleoside ribohydrolase
Comments: Also hydrolyses purine D-ribonucleosides, but more slowly. 2'-, 3'- and 5'-deoxynucleosides are not substrates [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37288-60-1
References:
1. Terada, M., Tatibana, M. and Hayaishi, O. Preparation and properties of nucleoside hydrolase from Pseudomonas fluorescens. J. Biol. Chem. 242 (1967) 5578-5585. [PMID: 12325375]
2. Petersen, C. and Møller, L.B. The RihA, RihB, and RihC ribonucleoside hydrolases of Escherichia coli. Substrate specificity, gene expression, and regulation. J. Biol. Chem. 276 (2001) 884-894. [PMID: 11027694]
3. Giabbai, B. and Degano, M. Cloning, purification, crystallization and X-ray analysis of the Escherichia coli pyrimidine nucleoside hydrolase YeiK. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 524-527. [PMID: 14993681]
4. Giabbai, B. and Degano, M. Crystal structure to 1.7 Å of the Escherichia coli pyrimidine nucleoside hydrolase YeiK, a novel candidate for cancer gene therapy. Structure 12 (2004) 739-749. [PMID: 15130467]
Accepted name: adenosylhomocysteine nucleosidase
Reaction: (1) S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
(2) 5'-deoxyadenosine + H2O = 5-deoxy-D-ribose + adenine
(3) S-methyl-5'-thioadenosine + H2O = 5-(methylsulfanyl)-D-ribose + adenine
For diagram of autoinducer AI-2 biosynthesis, click here and for diagram of the methionine-salvage pathway, click here
Other name(s): S-adenosylhomocysteine hydrolase (ambiguous); S-adenosylhomocysteine nucleosidase; 5'-methyladenosine nucleosidase; S-adenosylhomocysteine/5'-methylthioadenosine nucleosidase; AdoHcy/MTA nucleosidase; MTN2 (gene name); mtnN (gene name)
Systematic name: S-adenosyl-L-homocysteine homocysteinylribohydrolase
Comments: This enzyme, found in bacteria and plants, acts on three different substrates. It is involved in the S-adenosyl-L-methionine (SAM, AdoMet) cycle, which recycles S-adenosyl-L-homocysteine back to SAM, and in salvage pathways for 5'-deoxyadenosine and S-methyl-5'-thioadenosine, which are produced from SAM during the action of many enzymes. cf. the plant enzyme EC 3.2.2.16, methylthioadenosine nucleosidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9055-10-1
References:
1. Duerre, J.A. A hydrolytic nucleosidase acting on S-adenosylhomocysteine and on 5-methylthioadenosine. J. Biol. Chem. 237 (1962) 3737-3741.
2. Ferro, A.J., Barrett, A. and Shapiro, S.K. Kinetic properties and the effect of substrate analogues on 5'-methylthioadenosine nucleosidase from Escherichia coli. Biochim. Biophys. Acta 438 (1976) 487-494. [PMID: 782530]
3. Cornell, K.A., Swarts, W.E., Barry, R.D. and Riscoe, M.K. Characterization of recombinant Eschericha coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: analysis of enzymatic activity and substrate specificity. Biochem. Biophys. Res. Commun. 228 (1996) 724-732. [PMID: 8941345]
4. Park, E.Y., Choi, W.S., Oh, S.I., Kim, K.N., Shin, J.S. and Song, H.K. Biochemical and structural characterization of 5'-methylthioadenosine nucleosidases from Arabidopsis thaliana. Biochem. Biophys. Res. Commun. 381 (2009) 619-624. [PMID: 19249293]
5. Farrar, C.E., Siu, K.K., Howell, P.L. and Jarrett, J.T. Biotin synthase exhibits burst kinetics and multiple turnovers in the absence of inhibition by products and product-related biomolecules. Biochemistry 49 (2010) 9985-9996. [PMID: 20961145]
6. North, J.A., Wildenthal, J.A., Erb, T.J., Evans, B.S., Byerly, K.M., Gerlt, J.A. and Tabita, F.R. A bifunctional salvage pathway for two distinct S-adenosylmethionine by-products that is widespread in bacteria, including pathogenic Escherichia coli. Mol. Microbiol. (2020) . [PMID: 31950558]
Accepted name: pyrimidine-5'-nucleotide nucleosidase
Reaction: a pyrimidine 5'-nucleotide + H2O = D-ribose 5-phosphate + a pyrimidine base
Other name(s): pyrimidine nucleotide N-ribosidase; Pyr5N
Systematic name: pyrimidine-5'-nucleotide phosphoribo(deoxyribo)hydrolase
Comments: Also acts on dUMP, dTMP and dCMP.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9023-31-8
References:
1. Imada, A. Degradation of pyrimidine nucleotides by enzyme systems of Streptomyces. II. Pyrimidine 5'-nucleotide phosphoribo(deoxyribo) hydrolase of Streptomyces virginiae. J. Gen. Appl. Microbiol. 13 (1967) 267-278.
2. Imada, A., Kuno, M. and Igarasi, S. Degradation of pyrimidine nucleotides by enzyme systems of Streptomyces. I. Ribose-5-phosphate formation from pyrimidine nucleotides. J. Gen. Appl. Microbiol. 13 (1967) 255-265.
Accepted name: β-aspartyl-N-acetylglucosaminidase
Reaction: 1-β-aspartyl-N-acetyl-D-glucosaminylamine + H2O = L-asparagine + N-acetyl-D-glucosamine
Other name(s): β-aspartylacetylglucosaminidase
Systematic name: 1-β-aspartyl-N-acetyl-D-glucosaminylamine L-asparaginohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9027-31-0
References:
1. Eylar, E.H. and Murakami, M. β-Aspartyl-N-acetylglucosaminidase from epididymis. Methods Enzymol. 8 (1966) 597-600.
Accepted name: inosinate nucleosidase
Reaction: IMP + H2O = D-ribose 5-phosphate + hypoxanthine
For diagram click here.
Glossary: IMP = inosine 5'-phosphate
Other name(s): 5'-inosinate phosphoribohydrolase
Systematic name: IMP phosphoribohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37288-61-2
References:
1. Kuninaka, A. 5'-Inosinic acid-N-ribosidase in Aspergillus. Koso Kagaka Shinojiumu 12 (1957) 65-69.
Accepted name: 1-methyladenosine nucleosidase
Reaction: 1-methyladenosine + H2O = 1-methyladenine + D-ribose
Other name(s): 1-methyladenosine hydrolase
Systematic name: 1-methyladenosine ribohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37367-71-8
References:
1. Tarr, H.L.A. 1-Methyladenosine hydrolase of starfish (Pisaster ochraceous). J. Fish Res. Board Can. 30 (1973) 1861-1866.
Accepted name: NMN nucleosidase
Reaction: nicotinamide β-D-ribonucleotide + H2O = D-ribose 5-phosphate + nicotinamide
Other name(s): NMNase; nicotinamide mononucleotide nucleosidase; nicotinamide mononucleotidase; NMN glycohydrolase; NMNGhase
Systematic name: nicotinamide-nucleotide phosphoribohydrolase
Comments: The enzyme is thought to participate in an NAD+-salvage pathway. In eukaryotic organisms this activity has been attributed to EC 3.2.2.6, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37237-49-3
References:
1. Andreoli, A.J., Okita, T.W., Bloom, R. and Grover, T.A. The pyridine nucleotide cycle: presence of a nicotinamide mononucleotide-specific glycohydrolase in Escherichia coli. Biochem. Biophys. Res. Commun. 49 (1972) 264-269. [PMID: 4342726]
2. Imai, T. Isolation and properties of a glycohydrolase specific for nicotinamide mononucleotide from Azotobacter vinelandii. J. Biochem. 85 (1979) 887Ð899. [PMID: 457634]
3. Imai, T. Properties of allosteric nicotinamide mononucleotide glycohydrolase from Azotobacter vinelandii: activation and inhibition. J. Biochem. 101 (1987) 163Ð173. [PMID: 3571198]
Accepted name: DNA-deoxyinosine glycosylase
Reaction: Hydrolyses DNA and polynucleotides, releasing free hypoxanthine
Other name(s): DNA(hypoxanthine) glycohydrolase; deoxyribonucleic acid glycosylase; hypoxanthine-DNA glycosylase
Systematic name: DNA-deoxyinosine deoxyribohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 68247-62-1
References:
1. Karran, P. and Lindahl, T. Enzymatic excision of free hypoxanthine from polydeoxynucleotides and DNA containing deoxyinosine monophosphate residues. J. Biol. Chem. 253 (1978) 5877-5879. [PMID: 98523]
Accepted name: methylthioadenosine nucleosidase
Reaction: S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine
For diagram click here.
Other name(s): 5'-methylthioadenosine nucleosidase; MTA nucleosidase; MeSAdo nucleosidase; methylthioadenosine methylthioribohydrolase
Systematic name: S-methyl-5'-thioadenosine adeninehyrolase
Comments: Does not act on S-adenosylhomocysteine. cf. EC 3.2.2.9 adenosylhomocysteine nucleosidase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 50812-28-7
References:
1. Guranowski, A.B., Chiang, P.K. and Cantoni, G.L. 5'-Methylthioadenosine nucleosidase. Purification and characterization of the enzyme from Lupinus luteus seeds. Eur. J. Biochem. 114 (1981) 293-299. [PMID: 6783408]
Accepted name: deoxyribodipyrimidine endonucleosidase
Reaction: Cleaves the N-glycosidic bond between the 5'-pyrimidine residue in cyclobutadipyrimidine (in DNA) and the corresponding deoxy-D-ribose residue
Other name(s): pyrimidine dimer DNA-glycosylase; endonuclease V; deoxyribonucleate pyrimidine dimer glycosidase; pyrimidine dimer DNA glycosylase; T4-induced UV endonuclease; PD-DNA glycosylase
Systematic name: deoxy-D-ribocyclobutadipyrimidine polynucleotidodeoxyribohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 75302-33-9
References:
1. Haseltine, W.A., Gordon, L.K., Lindan, C.P., Grafstrom, R.H., Shaper, N.L. and Grossman, L. Cleavage of pyrimidine dimers in specific DNA sequences by a pyrimidine dimer DNA-glycosylase of M. luteus. Nature 285 (1980) 634-641. [PMID: 6248789]
[EC 3.2.2.18 Deleted entry: glycopeptide N-glycosidase. Now included with EC 3.5.1.52 N4-(β-N-acetylglucosaminyl)-L-asparaginase (EC 3.2.2.18 created 1984, deleted 1989)]
Accepted name: [protein ADP-ribosylarginine] hydrolase
Reaction: (1) protein-Nω-(ADP-D-ribosyl)-L-arginine + H2O = ADP-D-ribose + protein-L-arginine
(2) Nω-(ADP-D-ribosyl)-L-arginine + H2O = ADP-ribose + L-arginine
Other name(s): ADP-ribose-L-arginine cleavage enzyme; ADP-ribosylarginine hydrolase; Nω-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase
Systematic name: protein-Nω-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase
Comments: The enzyme will remove ADP-D-ribose from arginine residues in ADP-ribosylated proteins.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 98668-52-1
References:
1. Moss, J., Jacobson, M.K. and Stanley, S.J. Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-L-arginine cleavage enzyme. Proc. Natl. Acad. Sci. USA 82 (1985) 5603-5607. [PMID: 2994036]
2. Moss, J., Stanley, S.J., Nightingale, M.S., Murtagh, J.J., Jr., Monaco, L., Mishima, K., Chen, H.C., Williamson, K.C. and Tsai, S.C. Molecular and immunological characterization of ADP-ribosylarginine hydrolases. J. Biol. Chem. 267 (1992) 10481-10488. [PMID: 1375222]
3. Konczalik, P. and Moss, J. Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases. J. Biol. Chem. 274 (1999) 16736-16740. [PMID: 10358013]
4. Takada, T., Iida, K. and Moss, J. Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase. J. Biol. Chem. 268 (1993) 17837-17843 [PMID: 8349667]
5. Ohno, T., Tsuchiya, M., Osago, H., Hara, N., Jidoi, J. and Shimoyama, M. Detection of arginine-ADP-ribosylated protein using recombinant ADP-ribosylarginine hydrolase. Anal. Biochem. 10 (1995) 115-122 [PMID: 8678289]
Accepted name: DNA-3-methyladenine glycosylase I
Reaction: Hydrolysis of alkylated DNA, releasing 3-methyladenine
Other name(s): deoxyribonucleate 3-methyladenine glycosidase I; 3-methyladenine DNA glycosylase I; DNA-3-methyladenine glycosidase I
Systematic name: alkylated-DNA glycohydrolase (releasing methyladenine and methylguanine)
Comments: Involved in the removal of alkylated bases from DNA in Escherichia coli (cf. EC 2.1.1.63 methylated-DNA—[protein]-cysteine S-methyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 89287-37-6
References:
1. Evensen, G. and Seeberg, E. Adaptation to alkylation resistance involves the induction of a DNA glycosylase. Nature 296 (1982) 773-775. [PMID: 7040984]
2. Karran, P., Hjelmgren, T. and Lindahl, T. Induction of a DNA glycosylase for N-methylated purines is part of the adaptive response to alkylating agents. Nature 296 (1982) 770-773. [PMID: 7040983]
3. Thomas, L., Yang, C.-H. and Goldthwait, D.A. Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine. Biochemistry 21 (1982) 1162-1169. [PMID: 7041972]
Accepted name: DNA-3-methyladenine glycosylase II
Reaction: Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine
Other name(s): deoxyribonucleate 3-methyladenine glycosidase II; 3-methyladenine DNA glycosylase II; DNA-3-methyladenine glycosidase II; AlkA
Systematic name: alkylated-DNA glycohydrolase (releasing methyladenine and methylguanine)
Comments: Involved in the removal of alkylated bases from DNA in Escherichia coli (cf. EC 2.1.1.63 methylated-DNA—[protein]-cysteine S-methyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 89287-38-7
References:
1. Evensen, G. and Seeberg, E. Adaptation to alkylation resistance involves the induction of a DNA glycosylase. Nature 296 (1982) 773-775. [PMID: 7040984]
2. Karran, P., Hjelmgren, T. and Lindahl, T. Induction of a DNA glycosylase for N-methylated purines is part of the adaptive response to alkylating agents. Nature 296 (1982) 770-773. [PMID: 7040983]
3. Riazuddin, S. and Lindahl, T. Properties of 3-methyladenine-DNA glycosylase from Escherichia coli. Biochemistry 17 (1978) 2110-2118. [PMID: 352392]
4. Thomas, L., Yang, C.-H. and Goldthwait, D.A. Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine. Biochemistry 21 (1982) 1162-1169. [PMID: 7041972]
Accepted name: rRNA N-glycosylase
Reaction: Hydrolysis of the N-glycosylic bond at A-4324 in 28S rRNA from rat ribosomes
Other name(s): ribosomal ribonucleate N-glycosidase; nigrin b; RNA N-glycosidase; rRNA N-glycosidase; ricin; momorcochin-S; Mirabilis antiviral protein; momorcochin-S; gelonin; saporins
Systematic name: rRNA N-glycohydrolase
Comments: Ricin A-chain and related toxins show this activity. Naked rRNA is attacked more slowly than rRNA in intact ribosomes. Naked rRNA from Escherichia coli is cleaved at a corresponding position.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 113756-12-0
References:
1. Endo, Y. and Tsurugi, K. The RNA N-glycosidase activity of ricin A-chain. The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA. J. Biol. Chem. 263 (1988) 8735-8739. [PMID: 3288622]
Accepted name: DNA-formamidopyrimidine glycosylase
Reaction: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
Other name(s): Fapy-DNA glycosylase; deoxyribonucleate glycosidase; 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase; 2,6-diamino-4-hydroxy-5(N-methyl)formamidopyrimidine-DNA glycosylase; formamidopyrimidine-DNA glycosylase; DNA-formamidopyrimidine glycosidase; Fpg protein
Systematic name: DNA glycohydrolase [2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimide releasing]
Comments: May play a significant role in processes leading to recovery from mutagenesis and/or cell death by alkylating agents. Also involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 78783-53-6
References:
1. Boiteux, S., O'Connor, T.R. and Laval J. Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and sequencing of the fpg structural gene and overproduction of the protein. EMBO J. 6 (1987) 3177-3183. [PMID: 3319582]
Accepted name: ADP-ribosyl-[dinitrogen reductase] hydrolase
Reaction: [dinitrogen reductase]-Nω-α-(ADP-D-ribosyl)-L-arginine + H2O = ADP-D-ribose + [dinitrogen reductase]-L-arginine
Other name(s): azoferredoxin glycosidase; azoferredoxin-activating enzymes; dinitrogenase reductase-activating glycohydrolase; ADP-ribosyl glycohydrolase; draG (gene name)
Systematic name: ADP-D-ribosyl-[dinitrogen reductase] ADP-ribosylhydrolase
Comments: The enzyme restores the activity of EC 1.18.6.1, nitrogenase, by catalysing the removal of ADP-ribose from an arginine residue of the dinitrogenase reductase component of nitrogenase. This activity occurs only when the nitrogenase product, ammonium, is not available. The combined activity of this enzyme and EC 2.4.2.37, NAD+-dinitrogen–reductase ADP-D-ribosyltransferase, controls the level of activity of nitrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 125626-63-3
References:
1. Fitzmaurice, W.P., Saari, L.L., Lowery, R.G., Ludden, P.W. and Roberts, G.P. Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum. Mol. Gen. Genet. 218 (1989) 340-347. [PMID: 2506427]
2. Li, X.D., Huergo, L.F., Gasperina, A., Pedrosa, F.O., Merrick, M. and Winkler, F.K. Crystal structure of dinitrogenase reductase-activating glycohydrolase (DraG) reveals conservation in the ADP-ribosylhydrolase fold and specific features in the ADP-ribose-binding pocket. J. Mol. Biol. 390 (2009) 737-746. [PMID: 19477184]
3. Berthold, C.L., Wang, H., Nordlund, S. and Hogbom, M. Mechanism of ADP-ribosylation removal revealed by the structure and ligand complexes of the dimanganese mono-ADP-ribosylhydrolase DraG. Proc. Natl. Acad. Sci. USA 106 (2009) 14247-14252. [PMID: 19706507]
Accepted name: N-methyl nucleosidase
Reaction: 7-methylxanthosine + H2O = 7-methylxanthine + D-ribose
For diagram of reaction click here
Other name(s): 7-methylxanthosine nucleosidase; N-MeNase; N-methyl nucleoside hydrolase; methylpurine nucleosidase
Systematic name: 7-methylxanthosine ribohydrolase
Comments: The enzyme preferentially hydrolyses 3- and 7-methylpurine nucleosides, such as 3-methylxanthosine, 3-methyladenosine and 7-methylguanosine. Hydrolysis of 7-methylxanthosine to form 7-methylxanthine is the second step in the caffeine-biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1.Negishi, O., Ozawa, T. and Imagawa, H. N-Methyl nucleosidase from tea leaves. Agric. Biol. Chem. 52 (1988) 169-175.
Accepted name: futalosine hydrolase
Reaction: futalosine + H2O = dehypoxanthine futalosine + hypoxanthine
For diagram of reaction click here.
Glossary: futalosine = 3-(3-((3S,4R)-3,4-dihydroxy-5-(6-oxo-3H-purin-9(6H)-yl)tetrahydrofuran-2-yl)propanoyl)benzoate
dehypoxanthine futalosine = 7-(3-carboxyphenyl)-D-ribo-7-dehydro-5,6-dideoxyheptose
Other name(s): futalosine nucleosidase; MqnB (ambiguous)
Systematic name: futalosine ribohydrolase
Comments: This enzyme, which is specific for futalosine, catalyses the second step of a novel menaquinone biosynthetic pathway that is found in some prokaryotes.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number:
References:
1. Hiratsuka, T., Furihata, K., Ishikawa, J., Yamashita, H., Itoh, N., Seto, H. and Dairi, T. An alternative menaquinone biosynthetic pathway operating in microorganisms. Science 321 (2008) 1670-1673. [PMID: 18801996]
Accepted name: uracil-DNA glycosylase
Reaction: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil
Other name(s): UdgB (ambiguous); uracil-DNA N-glycosylase; UDG (ambiguous); uracil DNA glycohydrolase
Systematic name: uracil-DNA deoxyribohydrolase (uracil-releasing)
Comments: Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. EC 3.2.2.27 and double-stranded uracil-DNA glycosylase (EC 3.2.2.28) form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolysing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalysing the removal of mis-incorporated uracil from DNA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Lee, M.S., Kim, G.A., Seo, M.S., Lee, J.H. and Kwon, S.T. Characterization of heat-labile uracil-DNA glycosylase from Psychrobacter sp. HJ147 and its application to the polymerase chain reaction. Biotechnol. Appl. Biochem. 52 (2009) 167-175. [PMID: 18412541]
2. Kim, G.A., Lee, M.S., Sun, Y., Lee, B.D., Lee, J.I., Lee, J.H. and Kwon, S.T. Characterization of cold-active uracil-DNA glycosylase from Bacillus sp. HJ171 and its use for contamination control in PCR. Appl. Microbiol. Biotechnol. 80 (2008) 785-794. [PMID: 18626641]
3. Parikh, S.S., Putnam, C.D. and Tainer, J.A. Lessons learned from structural results on uracil-DNA glycosylase. Mutat Res 460 (2000) 183-199. [PMID: 10946228]
4. Stivers, J.T. and Drohat, A.C. Uracil DNA glycosylase: insights from a master catalyst. Arch. Biochem. Biophys. 396 (2001) 1-9. [PMID: 11716455]
Accepted name: double-stranded uracil-DNA glycosylase
Reaction: Specifically hydrolyzes mismatched double-stranded DNA and polynucleotides, releasing free uracil
Other name(s): Mug; double-strand uracil-DNA glycosylase; Dug; dsUDG; double-stranded DNA specific UDG; dsDNA specific UDG; UdgB (ambiguous); G:T/U mismatch-specific DNA glycosylase; UDG (ambiguous)
Systematic name: uracil-double-stranded DNA deoxyribohydrolase (uracil-releasing)
Comments: No activity on DNA containing a T/G mispair or single-stranded DNA containing either a site-specific uracil or 3,N4-ethenocytosine residue [2], significant role for double-stranded uracil-DNA glycosylase in mutation avoidance in non-dividing E. coli [3]. Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. Uracil-DNA glycosylase (EC 3.2.2.27) and EC 3.2.2.28 form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolysing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalysing the removal of mis-incorporated uracil from DNA.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Barrett, T.E., Scharer, O.D., Savva, R., Brown, T., Jiricny, J., Verdine, G.L. and Pearl, L.H. Crystal structure of a thwarted mismatch glycosylase DNA repair complex. EMBO J. 18 (1999) 6599-6609. [PMID: 10581234]
2. Sung, J.S. and Mosbaugh, D.W. Escherichia coli double-strand uracil-DNA glycosylase: involvement in uracil-mediated DNA base excision repair and stimulation of activity by endonuclease IV. Biochemistry 39 (2000) 10224-10235. [PMID: 10956012]
3. Mokkapati, S.K., Fernandez de Henestrosa, A.R. and Bhagwat, A.S. Escherichia coli DNA glycosylase Mug: a growth-regulated enzyme required for mutation avoidance in stationary-phase cells. Mol. Microbiol. 41 (2001) 1101-1111. [PMID: 11555290]
Accepted name: thymine-DNA glycosylase
Reaction: Hydrolyzes mismatched double-stranded DNA and polynucleotides, releasing free thymine
Other name(s): mismatch-specific thymine-DNA glycosylase; mismatch-specific thymine-DNA N-glycosylase; hTDG; hsTDG; TDG; thymine DNA glycosylase; G/T glycosylase; uracil/thymine DNA glycosylase; T:G mismatch-specific thymidine-DNA glycosylase; G:T mismatch-specific thymine DNA-glycosylase
Systematic name: thymine-DNA deoxyribohydrolase (thymine-releasing)
Comments: Thymine-DNA glycosylase is part of the DNA-repair machinery. Thymine removal is fastest when it is from a G/T mismatch with a 5'-flanking C/G pair. The glycosylase removes uracil from G/U, C/U, and T/U base pairs faster than it removes thymine from G/T [3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Waters, T.R. and Swann, P.F. Thymine-DNA glycosylase and G to A transition mutations at CpG sites. Mutat Res 462 (2000) 137-147. [PMID: 10767625]
2. Neddermann, P. and Jiricny, J. The purification of a mismatch-specific thymine-DNA glycosylase from HeLa cells. J. Biol. Chem. 268 (1993) 21218-21224. [PMID: 8407958]
3. Waters, T.R. and Swann, P.F. Kinetics of the action of thymine DNA glycosylase. J. Biol. Chem. 273 (1998) 20007-20014. [PMID: 9685338]
Accepted name: aminodeoxyfutalosine nucleosidase
Reaction: 6-amino-6-deoxyfutalosine + H2O = dehypoxanthine futalosine + adenine
For diagram of reaction click here.
Glossary: 6-amino-6-deoxyfutalosine = 3-{3-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]propanoyl}benzoate
dehypoxanthine futalosine = 3-{3-[(2R,3S,4R)-3,4,5-trihydroxytetrahydrofuran-2-yl]propanoyl}benzoate
Other name(s): AFL nucleosidase; aminofutalosine nucleosidase; methylthioadenosine nucleosidase; MqnB (ambiguous)
Systematic name: 6-amino-6-deoxyfutalosine ribohydrolase
Comments: The enzyme, found in several bacterial species, catalyses a step in a modified futalosine pathway for menaquinone biosynthesis. While the enzyme from some organisms also has the activity of EC 3.2.2.9, adenosylhomocysteine nucleosidase, the enzyme from Chlamydia trachomatis is specific for 6-amino-6-deoxyfutalosine [7].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Hiratsuka, T., Furihata, K., Ishikawa, J., Yamashita, H., Itoh, N., Seto, H. and Dairi, T. An alternative menaquinone biosynthetic pathway operating in microorganisms. Science 321 (2008) 1670-1673. [PMID: 18801996]
2. Li, X., Apel, D., Gaynor, E.C. and Tanner, M.E. 5'-methylthioadenosine nucleosidase is implicated in playing a key role in a modified futalosine pathway for menaquinone biosynthesis in Campylobacter jejuni. J. Biol. Chem. 286 (2011) 19392-19398. [PMID: 21489995]
3. Arakawa, C., Kuratsu, M., Furihata, K., Hiratsuka, T., Itoh, N., Seto, H. and Dairi, T. Diversity of the early step of the futalosine pathway. Antimicrob. Agents Chemother. 55 (2011) 913-916. [PMID: 21098241]
4. Wang, S., Haapalainen, A.M., Yan, F., Du, Q., Tyler, P.C., Evans, G.B., Rinaldo-Matthis, A., Brown, R.L., Norris, G.E., Almo, S.C. and Schramm, V.L. A picomolar transition state analogue inhibitor of MTAN as a specific antibiotic for Helicobacter pylori. Biochemistry 51 (2012) 6892-6894. [PMID: 22891633]
5. Mishra, V. and Ronning, D.R. Crystal structures of the Helicobacter pylori MTAN enzyme reveal specific interactions between S-adenosylhomocysteine and the 5'-alkylthio binding subsite. Biochemistry 51 (2012) 9763-9772. [PMID: 23148563]
6. Kim, R.Q., Offen, W.A., Davies, G.J. and Stubbs, K.A. Structural enzymology of Helicobacter pylori methylthioadenosine nucleosidase in the futalosine pathway. Acta Crystallogr. D Biol. Crystallogr. 70 (2014) 177-185. [PMID: 24419390]
7. Barta, M.L., Thomas, K., Yuan, H., Lovell, S., Battaile, K.P., Schramm, V.L. and Hefty, P.S. Structural and biochemical characterization of Chlamydia trachomatis hypothetical protein CT263 supports that menaquinone synthesis occurs through the futalosine pathway. J. Biol. Chem. 289 (2014) 32214-32229. [PMID: 25253688]
Accepted name: adenine glycosylase
Reaction: Hydrolyses free adenine bases from 7,8-dihydro-8-oxoguanine:adenine mismatched double-stranded DNA, leaving an apurinic site.
Other name(s): mutY (gene name); A/G-specific adenine glycosylase
Systematic name: adenine-DNA deoxyribohydrolase (adenine-releasing)
Comments: The enzyme serves as a mismatch repair enzyme that works to correct 7,8-dihydro-8-oxoguanine:adenine mispairs that arise in DNA when error-prone synthesis occurs past 7,8-dihydro-8-oxoguanine (GO) lesions in DNA. The enzyme excises the adenine of the mispair, producing an apurinic site sensitive to AP endonuclease activity. After removing the undamaged adenine the enzyme remains bound to the site to prevent EC 3.2.2.23 (MutM) from removing the GO lesion, which could lead to a double strand break. In vitro the enzyme is also active with adenine:guanine, adenine:cytosine, and adenine:7,8-dihydro-8-oxoadenine (AO) mispairs, removing the adenine in all cases.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Au, K.G., Clark, S., Miller, J.H. and Modrich, P. Escherichia coli mutY gene encodes an adenine glycosylase active on G-A mispairs. Proc. Natl. Acad. Sci. USA 86 (1989) 8877-8881. [PMID: 2682664]
2. Michaels, M.L., Tchou, J., Grollman, A.P. and Miller, J.H. A repair system for 8-oxo-7,8-dihydrodeoxyguanine. Biochemistry 31 (1992) 10964-10968. [PMID: 1445834]
[EC 3.2.3.1 Transferred entry: now EC 3.2.1.147 thioglucosidase (EC 3.2.3.1 created 1972, deleted 2001)]