Amidase

From Wikipedia, the free encyclopedia

In enzymology, an amidase (EC 3.5.1.4) is an enzyme that catalyzes the chemical reaction

a monocarboxylic acid amide + H₂O $\rightleftharpoons$ a monocarboxylate + NH₃

Thus, the two substrates of this enzyme are monocarboxylic acid amide and H₂O, whereas its two products are monocarboxylate and NH₃.

This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is acylamide amidohydrolase. Other names in common use include acylamidase, acylase, amidohydrolase, deaminase, fatty acylamidase, and N-acetylaminohydrolase. This enzyme participates in 6 metabolic pathways: urea cycle and metabolism of amino groups, phenylalanine metabolism, tryptophan metabolism, cyanoamino acid metabolism, benzoate degradation via coa ligation, and styrene degradation.

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

[edit] Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2PLQ and 2UXY.

[edit] References

IUBMB entry for 3.5.1.4
BRENDA references for 3.5.1.4 (Recommended.)
PubMed references for 3.5.1.4
PubMed Central references for 3.5.1.4
Google Scholar references for 3.5.1.4
Bray HG, James SP, Raffan IM, Ryman BE and Thorpe WV (1949). "The fate of certain organic acids and amides in the rabbit. 7. An amidase of rabbit liver". Biochem. J. 44: 618–625.
Bray HG, James SP, Thorpe WV and Wasdell MR (1950). "The fate of certain organic acids and amides in the rabbit. 11 Further observations on the hydrolysis of amides by tissue extracts". Biochem. J. 47: 294–299.