Adenosine-phosphate deaminase
From Wikipedia, the free encyclopedia
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.
[edit] References
- IUBMB entry for 3.5.4.17
- BRENDA references for 3.5.4.17 (Recommended.)
- PubMed references for 3.5.4.17
- PubMed Central references for 3.5.4.17
- Google Scholar references for 3.5.4.17
- Su JC, Li CC, Ting CC (1966). "A new adenylate deaminase from red marine alga Porphyra crispata". Biochemistry. 5: 536–43. PMID 5940938.
- Yates MG (1969). "A non-specific adenine nucleotide deaminase from desulfovibrio desulfuricans". Biochim. Biophys. Acta. 171: 299–310. PMID 5773435.
[edit] External links
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- The CAS registry number for this enzyme class is 37289-20-6.