Adenosine-phosphate deaminase
Appearance
adenosine-phosphate deaminase | |||||||||
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Identifiers | |||||||||
EC no. | 3.5.4.17 | ||||||||
CAS no. | 37289-20-6 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, an adenosine-phosphate deaminase (EC 3.5.4.17) is an enzyme that catalyzes the chemical reaction
- 5'-AMP + H2O 5'-IMP + NH3
Thus, the two substrates of this enzyme are 5'-AMP and H2O, whereas its two products are 5'-IMP and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is adenosine-phosphate aminohydrolase. Other names in common use include adenylate deaminase, adenine nucleotide deaminase, and adenosine (phosphate) deaminase.
References
- Su JC, Li CC, Ting CC (1966). "A new adenylate deaminase from red marine alga Porphyra crispata". Biochemistry. 5 (2): 536–43. doi:10.1021/bi00866a020. PMID 5940938.
- Yates MG (1969). "A non-specific adenine nucleotide deaminase from desulfovibrio desulfuricans". Biochim. Biophys. Acta. 171 (2): 299–310. doi:10.1016/0005-2744(69)90163-6. PMID 5773435.