Agmatine deiminase

In enzymology, an agmatine deiminase (EC 3.5.3.12) is an enzyme that catalyzes the chemical reaction

agmatine + H2O N-carbamoylputrescine + NH3
agmatine deiminase
Identifiers
EC number3.5.3.12
CAS number37289-17-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Thus, the two substrates of this enzyme are agmatine and H2O, whereas its two products are N-carbamoylputrescine and NH3.

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 agmatine iminohydrolase. This enzyme is also called agmatine amidinohydrolase. This enzyme participates in urea cycle and metabolism of amino groups.

Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1VKP, 2EWO, 2JER, and 2Q3U.

gollark: Why specifically *those*?
gollark: If you just define anything which happens as being part of the balance retroactively, then it is not meaningful to complain about it.
gollark: Well, it's a thing which happens in nature.
gollark: There was an experiment which wanted to demonstrate group selection. They put flies that in an environment with limited resources which could only support so many fly children. If nature was nice and kind, they would magically turn down their breeding. As is quite obvious in retrospect, evolutionary processes would *never do this* and they cannibalized each other's young.
gollark: There are nasty things like those various parasitic wasps.

References

    • Smith TA (1969). "Agmatine iminohydrolase in maize". Phytochemistry. 8 (11): 2111–2117. doi:10.1016/S0031-9422(00)88168-6.
    • Srivenugopal KS, Adiga PR (1981). "Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase)". J. Biol. Chem. 256 (18): 9532–41. PMID 6895223.


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