Agmatinase

In enzymology, an agmatinase (EC 3.5.3.11) is an enzyme that catalyzes the chemical reaction

agmatine + H₂O <math>\rightleftharpoons</math> putrescine + urea

Thus, the two substrates of this enzyme are agmatine and H₂O, whereas its two products are putrescine and urea.

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 amidinohydrolase. Other names in common use include agmatine ureohydrolase, and SpeB. This enzyme participates in urea cycle and metabolism of amino groups.

Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1GQ6, 1GQ7, 1WOG, 1WOH, and 1WOI.

References

IUBMB entry for 3.5.3.11
BRENDA references for 3.5.3.11 (Recommended.)
PubMed references for 3.5.3.11
PubMed Central references for 3.5.3.11
Google Scholar references for 3.5.3.11
Hirshfield IN, Rosenfeld HJ, Leifer Z, Maas WK (1970). "Isolation and characterization of a mutant of Escherichia coli blocked in the synthesis of putrescine". J. Bacteriol. 101: 725–30. PMID 4908780.
Vicente C and Legaz ME (1982). "Preparation and properties of agmatine amidinohydrolase of Evernia prunastri". Physiol. Plant. 55: 335–339.