The Enzyme Database

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EC 2.4.99.20     
Accepted name: 2′-phospho-ADP-ribosyl cyclase/2′-phospho-cyclic-ADP-ribose transferase
Reaction: NADP+ + nicotinate = nicotinate-adenine dinucleotide phosphate + nicotinamide (overall reaction)
(1a) NADP+ = 2′-phospho-cyclic ADP-ribose + nicotinamide
(1b) 2′-phospho-cyclic ADP-ribose + nicotinate = nicotinate-adenine dinucleotide phosphate
For diagram of cyclic ADP-ribose biosynthesis, click here
Glossary: 2′-phospho-cyclic ADP-ribose = cADPRP
nicotinic acid-adenine dinucleotide phosphate = NAADP+
Other name(s): diphosphopyridine nucleosidase (ambiguous); CD38 (gene name); BST1 (gene name)
Systematic name: NADP+:nicotinate ADP-ribosyltransferase
Comments: This multiunctional enzyme catalyses both the removal of nicotinamide from NADP+, forming 2′-phospho-cyclic ADP-ribose, and the addition of nicotinate to the cyclic product, forming NAADP+, 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 3.2.2.6, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Chini, E.N., Chini, C.C., Kato, I., Takasawa, S. and Okamoto, H. CD38 is the major enzyme responsible for synthesis of nicotinic acid-adenine dinucleotide phosphate in mammalian tissues. Biochem. J. 362 (2002) 125–130. [PMID: 11829748]
2.  Moreschi, I., Bruzzone, S., Melone, L., De Flora, A. and Zocchi, E. NAADP+ synthesis from cADPRP and nicotinic acid by ADP-ribosyl cyclases. Biochem. Biophys. Res. Commun. 345 (2006) 573–580. [DOI] [PMID: 16690024]
[EC 2.4.99.20 created 2014]
 
 
EC 3.2.2.5     
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); NAD+ nucleosidase
Systematic name: NAD+ glycohydrolase
Comments: This enzyme catalyses the hydrolysis of NAD+, without associated ADP-ribosyl cyclase activity (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, 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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 21300288]
[EC 3.2.2.5 created 1961, modified 2013]
 
 
EC 3.2.2.6     
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 cyclic ADP-ribose biosynthesis, 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 acts on NAD+, catalysing 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) 928–937. [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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 16154090]
[EC 3.2.2.6 created 1961, modified 2004, modified 2014, modified 2018]
 
 
EC 3.2.2.14     
Accepted name: NMN nucleosidase
Reaction: β-nicotinamide 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. [DOI] [PMID: 4342726]
2.  Imai, T. Isolation and properties of a glycohydrolase specific for nicotinamide mononucleotide from Azotobacter vinelandii. J. Biochem. 85 (1979) 887–899. [PMID: 457634]
3.  Imai, T. Properties of allosteric nicotinamide mononucleotide glycohydrolase from Azotobacter vinelandii: activation and inhibition. J. Biochem. 101 (1987) 163–173. [PMID: 3571198]
[EC 3.2.2.14 created 1976, modified 2018]
 
 
EC 3.6.1.53     
Accepted name: Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase
Reaction: (1) CDP-choline + H2O = CMP + phosphocholine
(2) ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate
Other name(s): Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase; ADPRibase-Mn
Systematic name: CDP-choline phosphohydrolase
Comments: Requires Mn2+. Unlike EC 3.6.1.13, ADP-ribose diphosphatase, it cannot utilize Mg2+. ADP-D-ribose, CDP-choline, CDP-ethanolamine and ADP are substrates for this enzyme but ADP-D-glucose, UDP-D-glucose, CDP-D-glucose, CDP, CMP and AMP are not hydrolysed [2]. The mammalian enzyme hydrolyses cyclic ADP-ribose to 1-(5-phospho-β-D-ribosyl)-AMP with ~100-fold lower efficiency than ADP-D-ribose [3]. In rat, the enzyme is found predominantly in thymus and spleen.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Canales, J., Pinto, R.M., Costas, M.J., Hernández, M.T., Miró, A., Bernet, D., Fernández, A. and Cameselle, J.C. Rat liver nucleoside diphosphosugar or diphosphoalcohol pyrophosphatases different from nucleotide pyrophosphatase or phosphodiesterase I: substrate specificities of Mg2+-and/or Mn2+-dependent hydrolases acting on ADP-ribose. Biochim. Biophys. Acta 1246 (1995) 167–177. [DOI] [PMID: 7819284]
2.  Canales, J., Fernández, A., Ribeiro, J.M., Cabezas, A., Rodrigues, J.R., Cameselle, J.C. and Costas, M.J. Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase: a novel metallophosphoesterase family preferentially expressed in rodent immune cells. Biochem. J. 413 (2008) 103–113. [DOI] [PMID: 18352857]
3.  Canales, J., Fernandez, A., Rodrigues, J.R., Ferreira, R., Ribeiro, J.M., Cabezas, A., Costas, M.J. and Cameselle, J.C. Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn(2+)-dependent ADP-ribose/CDP-alcohol pyrophosphatase. FEBS Lett. 583 (2009) 1593–1598. [DOI] [PMID: 19379742]
4.  Rodrigues, J.R., Fernandez, A., Canales, J., Cabezas, A., Ribeiro, J.M., Costas, M.J. and Cameselle, J.C. Characterization of Danio rerio Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase, the structural prototype of the ADPRibase-Mn-like protein family. PLoS One 7:e42249 (2012). [DOI] [PMID: 22848751]
[EC 3.6.1.53 created 2008]
 
 


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