Biology:Agmatine deiminase
From HandWiki
Short description: InterPro Family
| agmatine deiminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.3.12 | ||||||||
| CAS number | 37289-17-1 | ||||||||
| 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 agmatine deiminase (EC 3.5.3.12) is an enzyme that catalyzes the chemical reaction
- agmatine + H2O [math]\displaystyle{ \rightleftharpoons }[/math] 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.
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.
References
- Smith TA (1969). "Agmatine iminohydrolase in maize". Phytochemistry 8 (11): 2111–2117. doi:10.1016/S0031-9422(00)88168-6.
- "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. 1981. PMID 6895223.
 |  |
