- Source: Allantoate deiminase
In enzymology, an allantoate deiminase (EC 3.5.3.9) is an enzyme that catalyzes the chemical reaction
allantoate + H2O
⇌
{\displaystyle \rightleftharpoons }
ureidoglycine + NH3 + CO2
Thus, the two substrates of this enzyme are allantoate and H2O, whereas its 3 products are ureidoglycine, NH3, and CO2.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is allantoate amidinohydrolase (decarboxylating). This enzyme is also called allantoate amidohydrolase. This enzyme participates in purine metabolism.
References
Vogels GD (February 1966). "Reversible activation of allantoate amidohydrolase by acid-pretreatment and other properties of the enzyme". Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation. 113 (2): 277–91. doi:10.1016/s0926-6593(66)80067-x. PMID 5328936.
