| Amidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 X-ray structure of native peptide amidase fromStenotrophomonas maltophilia at 1.4Å | |||||||||
| Identifiers | |||||||||
| Symbol | Amidase | ||||||||
| Pfam | PF01425 | ||||||||
| InterPro | IPR000120 | ||||||||
| PROSITE | PDOC00494 | ||||||||
| SCOP2 | 1ocm /SCOPe /SUPFAM | ||||||||
| OPM superfamily | 55 | ||||||||
| OPM protein | 1mt5 | ||||||||
| Membranome | 325 | ||||||||
| |||||||||
Inenzymology, anamidase (EC3.5.1.4,acylamidase,acylase (misleading),amidohydrolase (ambiguous),deaminase (ambiguous),fatty acylamidase,N-acetylaminohydrolase (ambiguous)) is anenzyme thatcatalyzes thehydrolysis of an amide. In this way, the twosubstrates of this enzyme are anamide andH2O, whereas its twoproducts are monocarboxylate andNH3.
This enzyme belongs to the family ofhydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. Thesystematic name of this enzyme class isacylamide amidohydrolase. Other names in common use includeacylamidase,acylase,amidohydrolase,deaminase,fatty acylamidase, andN-acetylaminohydrolase. This enzyme participates in 6metabolic pathways:urea cycle and metabolism of amino groups,phenylalanine metabolism,tryptophan metabolism,cyanoamino acid metabolism,benzoate degradation via coa ligation, andstyrene degradation.
Amidases contain aconserved stretch of approximately 130amino acids known as the ASsequence. They are widespread, being found in bothprokaryotes andeukaryotes. ASenzymescatalyse thehydrolysis ofamidebonds (CO-NH2), although the family has diverged widely with regard tosubstrate specificity and function. Nonetheless, these enzymes maintain a core alpha/beta/alpha structure, where the topologies of the N- and C-terminal halves are similar. AS enzymes characteristically have ahighly conserved C-terminal region rich inserine and glycine residues, but devoid ofaspartic acid andhistidine residues, therefore they differ from classical serinehydrolases. These enzymes possess a unique, highlyconserved Ser-Ser-Lyscatalytic triad used for amide hydrolysis, although thecatalytic mechanism for acyl-enzymeintermediate formation can differ between enzymes.[1]
Examples of AS signature-containing enzymes include:
 | This section needs to beupdated. Please help update this article to reflect recent events or newly available information.(May 2017) |
As of late 2018, 162structures have been solved for this family, which can be accessed at thePfamArchived 2021-09-18 at theWayback Machine.
