Amidase
| amidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| Amidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| OPM superfamily | 55 | ||||||||
| OPM protein | 1mt5 | ||||||||
| Membranome | 325 | ||||||||
| |||||||||
In
substrates of this enzyme are an amide and H2O, whereas its two products are monocarboxylate and NH3
.
This enzyme belongs to the family of
tryptophan metabolism, cyanoamino acid metabolism, benzoate degradation via coa ligation, and styrene degradation
.
Amidases contain a
highly conserved C-terminal region rich in serine and glycine residues, but devoid of aspartic acid and histidine residues, therefore they differ from classical serine hydrolases. These enzymes possess a unique, highly conserved Ser-Ser-Lys catalytic triad used for amide hydrolysis, although the catalytic mechanism for acyl-enzyme intermediate formation can differ between enzymes.[1]
Examples of AS signature-containing enzymes include:
- peptides.
- transmitters.
- Malonamidase E2,nitrogen metabolism.
- Subunit A of Glu-tRNA(Gln) amidotransferase,heterotrimeric enzyme that catalyses the formation of Gln-tRNA(Gln) by the transamidation of misacylated Glu-tRNA(Gln) via amidolysis of glutamine.
Structural studies
 | This section needs to be updated. (May 2017) |
As of late 2018, 162
structures have been solved for this family, which can be accessed at the Pfam Archived 2021-09-18 at the Wayback Machine
.
References
Further reading
- Bray HG, James SP, Raffan IM, Ryman BE, Thorpe WV (1949). "The fate of certain organic acids and amides in the rabbit. 7. An amidase of rabbit liver". Biochem. J. 44 (5): 618–625. PMC 1274617.
- Bray HG, James SP, Thorpe WV, 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 (3): 294–299. PMID 14800883.
