Biology:Diadenosine hexaphosphate hydrolase (AMP-forming)
From HandWiki
| Diadenosine hexaphosphate hydrolase (AMP-forming) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.6.1.60 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Diadenosine hexaphosphate hydrolase (AMP-forming) (EC 3.6.1.60, hAps1, NUDT11 (gene), hAps2, NUDT10 (gene)) is an enzyme with systematic name P1,P6-bis(5'-adenosyl)hexaphosphate nucleotidohydrolase (AMP-forming).[1][2] This enzyme catalyses the following chemical reaction
- (1) P1,P6-bis(5'-adenosyl)hexaphosphate + H2O [math]\displaystyle{ \rightleftharpoons }[/math] adenosine 5'-pentaphosphate + AMP
- (2) P1,P5-bis(5'-adenosyl)pentaphosphate + H2O [math]\displaystyle{ \rightleftharpoons }[/math] adenosine 5'-tetraphosphate + AMP
A divalent cation is essential for activity.
References
- ↑ "Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases". BMC Biochemistry 3: 20. July 2002. doi:10.1186/1471-2091-3-20. PMID 12121577.
- ↑ "The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type protein". The Journal of Biological Chemistry 274 (31): 21735–40. July 1999. doi:10.1074/jbc.274.31.21735. PMID 10419486.
External links
- Diadenosine+hexaphosphate+hydrolase+(AMP-forming) at the US National Library of Medicine Medical Subject Headings (MeSH)
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