Allantoate deiminase

allantoate deiminase
Identifiers
EC number 3.5.3.9
CAS number 37289-13-7
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

In enzymology, an allantoate deiminase (EC 3.5.3.9) is an enzyme that catalyzes the chemical reaction

allantoate + H2O 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 (1966). "Reversible activation of allantoate amidohydrolase by acid-pretreatment and other properties of the enzyme". Biochim. Biophys. Acta. 113 (2): 277&ndash, 91. doi:10.1016/s0926-6593(66)80067-x. PMID 5328936.


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