Pyrithiamine deaminase
From Wikipedia, the free encyclopedia
In enzymology, a pyrithiamine deaminase (EC 3.5.4.20) is an enzyme that catalyzes the chemical reaction
- 1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2- methylpyridinium bromide + H2O 1-(4-hydroxy-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2- methylpyridinium bromide + NH3
The 3 substrates of this enzyme are 1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-, methylpyridinium bromide, and H2O, whereas its 3 products are 1-(4-hydroxy-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-, methylpyridinium bromide, 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 1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-methy lpyridinium-bromide aminohydrolase.
[edit] References
- IUBMB entry for 3.5.4.20
- BRENDA references for 3.5.4.20 (Recommended.)
- PubMed references for 3.5.4.20
- PubMed Central references for 3.5.4.20
- Google Scholar references for 3.5.4.20
- Sinha AK, Chatterjee GC (1968). "Metabolism of pyrithiamine by the pyrithiamine-requiring mutant of Staphylococcus aureus". Biochem. J. 107: 165–9. PMID 5641872.
[edit] External links
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- The CAS registry number for this enzyme class is 37289-23-9.