Arginine deiminase explained

arginine deiminase
Ec Number:3.5.3.6
Cas Number:9027-98-9
Go Code:0016990

In enzymology, an arginine deiminase is an enzyme that catalyzes the chemical reaction

L-arginine + H2O

\rightleftharpoons

L-citrulline + NH3

Thus, the two substrates of this enzyme are L-arginine and H2O, whereas its two products are L-citrulline 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 L-arginine iminohydrolase. Other names in common use include arginine dihydrolase, citrulline iminase, and L-arginine deiminase. This enzyme participates in arginine and proline metabolism. This enzyme is widely expressed in bacteria, including streptococcus and actinomyces. The bacterial arginine deiminase expression could be regulated by various environmental factors.

Recently, a new enzyme that catalyzes the chemical reaction

L-arginine + 2H2O

\rightleftharpoons

L-ornithine + 2NH3 + CO2 was identified in cyanobacteria[1] which should be named as arginine dihydrolase.

Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes,,,,,, and .

References

  1. Zhang H, Liu YJ, Nie XQ, Liu LX, Hua Q, Zhao GP, Yang C . The cyanobacterial ornithine-ammonia cycle involves an arginine dihydrolase. . Nature Chemical Biology . 14 . 6 . 575–581 . April 2018 . 29632414 . 10.1038/s41589-018-0038-z . 4937151 .

This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Arginine deiminase".

Except where otherwise indicated, Everything.Explained.Today is © Copyright 2009-2024, A B Cryer, All Rights Reserved. Cookie policy.