The Enzyme Database

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EC 2.3.1.286     
Accepted name: protein acetyllysine N-acetyltransferase
Reaction: [protein]-N6-acetyl-L-lysine + NAD+ + H2O = [protein]-L-lysine + 2′′-O-acetyl-ADP-D-ribose + nicotinamide (overall reaction)
(1a) [protein]-N6-acetyl-L-lysine + NAD+ = [protein]-N6-[1,1-(5-adenosylyl-α-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
(1b) [protein]-N6-[1,1-(5-adenosylyl-α-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O = [protein]-L-lysine + 2′′-O-acetyl-ADP-D-ribose
Other name(s): Sir2; protein lysine deacetylase; NAD+-dependent protein deacetylase
Systematic name: [protein]-N6-acetyl-L-lysine:NAD+ N-acetyltransferase (NAD+-hydrolysing; 2′′-O-acetyl-ADP-D-ribose-forming)
Comments: The enzyme, found in all domains of life, is involved in gene regulation by deacetylating proteins. Some of the 2′′-O-acetyl-ADP-D-ribose converts non-enzymically to 3′′-O-acetyl-ADP-D-ribose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Landry, J., Slama, J.T. and Sternglanz, R. Role of NAD+ in the deacetylase activity of the SIR2-like proteins. Biochem. Biophys. Res. Commun. 278 (2000) 685–690. [PMID: 11095969]
2.  Sauve, A.A., Celic, I., Avalos, J., Deng, H., Boeke, J.D. and Schramm, V.L. Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions. Biochemistry 40 (2001) 15456–15463. [PMID: 11747420]
3.  Min, J., Landry, J., Sternglanz, R. and Xu, R.M. Crystal structure of a SIR2 homolog-NAD complex. Cell 105 (2001) 269–279. [PMID: 11336676]
4.  Jackson, M.D., Schmidt, M.T., Oppenheimer, N.J. and Denu, J.M. Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases. J. Biol. Chem. 278 (2003) 50985–50998. [PMID: 14522996]
5.  Sauve, A.A., Wolberger, C., Schramm, V.L. and Boeke, J.D. The biochemistry of sirtuins. Annu. Rev. Biochem. 75 (2006) 435–465. [PMID: 16756498]
[EC 2.3.1.286 created 2019]
 
 
EC 2.7.7.35     
Accepted name: ADP ribose phosphorylase
Reaction: ADP + D-ribose 5-phosphate = phosphate + ADP-D-ribose
Glossary: ADP-D-ribose = adenosine 5′-(5-deoxy-D-ribofuranos-5-yl diphosphate)
Other name(s): ; ribose-5-phosphate adenylyltransferase (ambiguous); adenosine diphosphoribose phosphorylase (ambiguous)
Systematic name: ADP:D-ribose-5-phosphate adenylyltransferase
Comments: The enzyme, characterized from the single-celled alga Euglena gracilis, catalyses an irreversible reaction in the direction of ADP formation. cf. EC 2.7.7.96, ADP-D-ribose pyrophosphorylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9054-55-1
References:
1.  Evans, W.R. and San Pietro, A. Phosphorolysis of adenosine diphosphoribose. Arch. Biochem. Biophys. 113 (1966) 236–244. [DOI] [PMID: 4287446]
2.  Stern, A.I. and Avron, M. An adenosine 5′-diphosphate ribose:orthophosphate adenylyltransferase from Euglena gracilis. Biochim. Biophys. Acta 118 (1966) 577–591. [PMID: 5970863]
[EC 2.7.7.35 created 1972, modified 2016]
 
 
EC 2.7.7.96     
Accepted name: ADP-D-ribose pyrophosphorylase
Reaction: ATP + D-ribose 5-phosphate = diphosphate + ADP-D-ribose
Other name(s): NUDIX5; NUDT5 (gene name); diphosphate—ADP-D-ribose adenylyltransferase; diphosphate adenylyltransferase (ambiguous)
Systematic name: ATP:D-ribose 5-phosphate adenylyltransferase
Comments: The human enzyme produces ATP in nuclei in situations of high energy demand, such as chromatin remodeling. The reaction is dependent on the presence of diphosphate. In its absence the enzyme catalyses the reaction of EC 3.6.1.13, ADP-ribose diphosphatase. cf. EC 2.7.7.35, ADP ribose phosphorylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wright, R.H., Lioutas, A., Le Dily, F., Soronellas, D., Pohl, A., Bonet, J., Nacht, A.S., Samino, S., Font-Mateu, J., Vicent, G.P., Wierer, M., Trabado, M.A., Schelhorn, C., Carolis, C., Macias, M.J., Yanes, O., Oliva, B. and Beato, M. ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for chromatin remodeling. Science 352 (2016) 1221–1225. [DOI] [PMID: 27257257]
[EC 2.7.7.96 created 2016]
 
 
EC 3.1.1.106     
Accepted name: O-acetyl-ADP-ribose deacetylase
Reaction: (1) 3′′-O-acetyl-ADP-D-ribose + H2O = ADP-D-ribose + acetate
(2) 2′′-O-acetyl-ADP-D-ribose + H2O = ADP-D-ribose + acetate
Other name(s): ymdB (gene name); MACROD1 (gene name)
Systematic name: O-acetyl-ADP-D-ribose carboxylesterase
Comments: The enzyme, characterized from the bacterium Escherichia coli and from human cells, removes the acetyl group from either the 2′′ or 3′′ position of O-acetyl-ADP-ribose, which are formed by the action of EC 2.3.1.286, protein acetyllysine N-acetyltransferase. The human enzyme can also remove ADP-D-ribose from phosphorylated double stranded DNA adducts.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Chen, D., Vollmar, M., Rossi, M.N., Phillips, C., Kraehenbuehl, R., Slade, D., Mehrotra, P.V., von Delft, F., Crosthwaite, S.K., Gileadi, O., Denu, J.M. and Ahel, I. Identification of macrodomain proteins as novel O-acetyl-ADP-ribose deacetylases. J. Biol. Chem. 286 (2011) 13261–13271. [PMID: 21257746]
2.  Zhang, W., Wang, C., Song, Y., Shao, C., Zhang, X. and Zang, J. Structural insights into the mechanism of Escherichia coli YmdB: A 2′-O-acetyl-ADP-ribose deacetylase. J. Struct. Biol. 192 (2015) 478–486. [PMID: 26481419]
3.  Agnew, T., Munnur, D., Crawford, K., Palazzo, L., Mikoc, A. and Ahel, I. MacroD1 is a promiscuous ADP-ribosyl hydrolase localized to mitochondria. Front. Microbiol. 9:20 (2018). [PMID: 29410655]
[EC 3.1.1.106 created 2019]
 
 
EC 3.1.3.84     
Accepted name: ADP-ribose 1′′-phosphate phosphatase
Reaction: ADP-D-ribose 1′′-phosphate + H2O = ADP-D-ribose + phosphate
Other name(s): POA1; Appr1p phosphatase; Poa1p; ADP-ribose 1′′-phosphate phosphohydrolase
Systematic name: ADP-D-ribose 1′′-phosphate phosphohydrolase
Comments: The enzyme is highly specific for ADP-D-ribose 1′′-phosphate. Involved together with EC 3.1.4.37, 2′,3′-cyclic-nucleotide 3′-phosphodiesterase, in the breakdown of adenosine diphosphate ribose 1′′,2′′-cyclic phosphate (Appr>p), a by-product of tRNA splicing.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shull, N.P., Spinelli, S.L. and Phizicky, E.M. A highly specific phosphatase that acts on ADP-ribose 1′′-phosphate, a metabolite of tRNA splicing in Saccharomyces cerevisiae. Nucleic Acids Res. 33 (2005) 650–660. [DOI] [PMID: 15684411]
[EC 3.1.3.84 created 2011]
 
 
EC 3.2.1.143     
Accepted name: poly(ADP-ribose) glycohydrolase
Reaction: hydrolyses poly(ADP-D-ribose) at glycosidic (1′′-2′) linkage of ribose-ribose bond to produce free ADP-D-ribose
For diagram of reaction, click here
Glossary: ADP-D-ribose = adenosine 5′-(5-deoxy-D-ribofuranos-5-yl diphosphate)
Comments: Specific to (1′′-2′) linkage of ribose-ribose bond of poly(ADP-D-ribose).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9068-16-0
References:
1.  Miwa, M. and Sugimura, T. Splitting of the ribose-ribose linkage of poly(adenosine diphosphate-ribose) by a calf thymus extract. J. Biol. Chem. 246 (1971) 6362–6364. [PMID: 4331388]
2.  Lin, W., Ame, J.C., Aboul-Ela, N., Jacobson, E.L. and Jacobson, M.K. Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase. J. Biol. Chem. 272 (1997) 11895–11901. [DOI] [PMID: 9115250]
[EC 3.2.1.143 created 2000]
 
 
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 3.2.2.19     
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-D-ribose + L-arginine
Glossary: ADP-D-ribose = adenosine 5′-(5-deoxy-D-ribofuranos-5-yl diphosphate)
Other name(s): ADP-ribose-L-arginine cleavage enzyme; ADP-ribosylarginine hydrolase; Nω-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase; protein-ω-N-(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, 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. [DOI] [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. [DOI] [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. [DOI] [PMID: 8678289]
[EC 3.2.2.19 created 1989, modified 2004]
 
 
EC 3.2.2.24     
Accepted name: ADP-ribosyl-[dinitrogen reductase] hydrolase
Reaction: [dinitrogen reductase]-Nω-α-(ADP-D-ribosyl)-L-arginine = 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, 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. [DOI] [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. [DOI] [PMID: 19706507]
[EC 3.2.2.24 created 1992]
 
 
EC 3.6.1.13     
Accepted name: ADP-ribose diphosphatase
Reaction: ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate
Glossary: ADP-D-ribose = adenosine 5′-(5-deoxy-D-ribofuranos-5-yl diphosphate)
Other name(s): ADPribose pyrophosphatase; adenosine diphosphoribose pyrophosphatase; ADPR-PPase; ADP-ribose ribophosphohydrolase
Systematic name: ADP-D-ribose ribophosphohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-83-3
References:
1.  Doherty, M.D. and Morrison, J.F. The hydrolysis of adenosine diphosphate ribose by a specific phosphohydrolase of rabbit-muscle extracts. Biochim. Biophys. Acta 65 (1962) 364–366. [DOI] [PMID: 14028386]
[EC 3.6.1.13 created 1965]
 
 
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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