Dimethylargininase

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In enzymology, a dimethylargininase (EC 3.5.3.18) is an enzyme that catalyzes the chemical reaction

Nomega,Nomega'-methyl-L-arginine + H₂O $\rightleftharpoons$ dimethylamine + L-citrulline

Thus, the two substrates of this enzyme are Nomega,Nomega'-methyl-L-arginine and H₂O, whereas its two products are dimethylamine and L-citrulline.

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 Nomega,Nomega'-methyl-L-arginine dimethylamidohydrolase. Other names in common use include dimethylarginine dimethylaminohydrolase, NG,NG-dimethylarginine dimethylaminohydrolase, NG,NG-dimethyl-L-arginine dimethylamidohydrolase, and omega,omega'-di-N-methyl-L-arginine dimethylamidohydrolase.

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

[edit] Structural studies

As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1H70, 2C6Z, 2CI1, 2CI3, 2CI4, 2CI5, 2CI6, 2CI7, 2JAI, and 2JAJ.