Allantoate deiminase

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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

  • IUBMB entry for 3.5.3.9
  • BRENDA references for 3.5.3.9 (Recommended.)
  • PubMed references for 3.5.3.9
  • PubMed Central references for 3.5.3.9
  • Google Scholar references for 3.5.3.9
  • Vogels GD (1966). "Reversible activation of allantoate amidohydrolase by acid-pretreatment and other properties of the enzyme". Biochim. Biophys. Acta. 113: 277&ndash, 91. PMID 5328936.

External links

The CAS registry number for this enzyme class is 37289-13-7.

Gene Ontology (GO) codes


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