Agmatine deiminase

From Wikipedia, the free encyclopedia

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

agmatine + H₂O $\rightleftharpoons$ N-carbamoylputrescine + NH₃

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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 3.5.3.12
BRENDA references for 3.5.3.12 (Recommended.)
PubMed references for 3.5.3.12
PubMed Central references for 3.5.3.12
Google Scholar references for 3.5.3.12
Smith TA (1969). "Agmatine iminohydrolase in maize". Phytochemistry 8: 2111–2117.
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: 9532–41. PMID 6895223.