Jump to content

Allantoate deiminase

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by Citation bot (talk | contribs) at 03:28, 25 May 2020 (Alter: journal. | You can use this bot yourself. Report bugs here. | Activated by AManWithNoPlan | All pages linked from User:AManWithNoPlan/sandbox2 | via #UCB_webform_linked). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

allantoate deiminase
Identifiers
EC no.3.5.3.9
CAS no.37289-13-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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 (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.