EC 3.2.2.5 - NAD+ glycohydrolase

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IntEnz Enzyme Nomenclature
EC 3.2.2.5

Names

Accepted name:
NAD+ glycohydrolase
Other names:
DPN hydrolase [ambiguous]
DPNase [ambiguous]
NAD glycohydrolase
NAD hydrolase [ambiguous]
NAD nucleosidase [ambiguous]
NADase [ambiguous]
diphosphopyridine nucleosidase [ambiguous]
nicotinamide adenine dinucleotide glycohydrolase [ambiguous]
nicotinamide adenine dinucleotide nucleosidase
ADP-ribosyl cyclase
β-NAD+ glycohydrolase
nga (gene name)
NAD+ nucleosidase
Systematic name:
NAD+ glycohydrolase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0061810
CAS Registry Number: 9032-65-9
UniProtKB/Swiss-Prot:

References

  1. Fehrenbach, F. J.
    [Purification and crystallization of NAD glycohydrolase of C streptococci]
    Eur. J. Biochem. 18: 94-102 (1971). [PMID: 4322210]
  2. Grushoff, P. S., Shany, S., Bernheimer, A. W.
    Purification and properties of streptococcal nicotinamide adenine dinucleotide glycohydrolase.
    J. Bacteriol. 122: 599-605 (1975). [PMID: 236282]
  3. Zhang, L., Xu, X., Luo, Z., Shen, D., Wu, H.
    Identification of an unusual AT(D)Pase-like activity in multifunctional NAD glycohydrolase from the venom of Agkistrodon acutus.
    Biochimie 91: 240-251 (2009). [PMID: 18952139]
  4. Ghosh, J., Anderson, P. J., Chandrasekaran, S., Caparon, M. G.
    Characterization of Streptococcus pyogenes beta-NAD+ glycohydrolase: re-evaluation of enzymatic properties associated with pathogenesis.
    J. Biol. Chem. 285: 5683-5694 (2010). [PMID: 20018886]
  5. Smith, C. L., Ghosh, J., Elam, J. S., Pinkner, J. S., Hultgren, S. J., Caparon, M. G., Ellenberger, T.
    Structural basis of Streptococcus pyogenes immunity to its NAD+ glycohydrolase toxin.
    Structure 19: 192-202 (2011). [PMID: 21300288]

[EC 3.2.2.5 created 1961, modified 2004, modified 2013]