Diadenosine hexaphosphate hydrolase (AMP-forming)
| Diadenosine hexaphosphate hydrolase (AMP-forming) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 | ||||||||
| |||||||||
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 adenosine 5'-pentaphosphate + AMP
- (2) P1,P5-bis(5'-adenosyl)pentaphosphate + H2O adenosine 5'-tetraphosphate + AMP
A divalent cation is essential for activity.
References
[edit]- ^ Leslie NR, McLennan AG, Safrany ST (July 2002). "Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases". BMC Biochemistry. 3: 20. doi:10.1186/1471-2091-3-20. PMC 117780. PMID 12121577.
- ^ Safrany ST, Ingram SW, Cartwright JL, Falck JR, McLennan AG, Barnes LD, Shears SB (July 1999). "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. doi:10.1074/jbc.274.31.21735. PMID 10419486.
External links
[edit]- Diadenosine+hexaphosphate+hydrolase+(AMP-forming) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
