| peptidyl-glutaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.43 | ||||||||
| CAS no. | 37228-70-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a peptidyl-glutaminase (EC 3.5.1.43) is an enzyme that catalyzes the chemical reaction
- alpha-N-peptidyl-L-glutamine + H2O alpha-N-peptidyl-L-glutamate + NH3
alpha-N-peptidyl-L-glutamate + NH3Thus, the two substrates of this enzyme are alpha-N-peptidyl-L-glutamine and H2O, whereas its two products are alpha-N-peptidyl-L-glutamate 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 peptidyl-L-glutamine amidohydrolase. Other names in common use include peptidoglutaminase I, peptideglutaminase, and peptidoglutaminase.
References
- Kikuchi M, Hayashida H, Nakano E, Sakaguchi K (1971). "Peptidoglutaminase. Enzymes for selective deamidation of gamma-amide of peptide-bound glutamine". Biochemistry. 10 (7): 1222–9. doi:10.1021/bi00783a019. PMID 4928623.
| Hydrolases: carbon-nitrogen non-peptide (EC 3.5) | |
|---|---|
| 3.5.1: Linear amides / Amidohydrolases | |
| 3.5.2: Cyclic amides/ Amidohydrolases | |
| 3.5.3: Linear amidines/ Ureohydrolases | |
| 3.5.4: Cyclic amidines/ Aminohydrolases | |
| 3.5.5: Nitriles/ Aminohydrolases | |
| 3.5.99: Other | |
| Enzymes | |
|---|---|
| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
|
This EC 3.5 enzyme-related article is a stub. You can help Misplaced Pages by expanding it. |