In enzymology, a 1-pyrroline-4-hydroxy-2-carboxylate deaminase (EC 3.5.4.22) is an enzyme that catalyzes the chemical reaction
| 1-pyrroline-4-hydroxy-2-carboxylate deaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.4.22 | ||||||||
| CAS no. | 9054-77-7 | ||||||||
| 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 | ||||||||
| |||||||||
- 1-pyrroline-4-hydroxy-2-carboxylate + H2O 2,5-dioxopentanoate + NH3
Thus, the two substrates of this enzyme are 1-pyrroline-4-hydroxy-2-carboxylate and H2O, whereas its two products are 2,5-dioxopentanoate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 1-pyrroline-4-hydroxy-2-carboxylate aminohydrolase (decyclizing). This enzyme is also called HPC deaminase. This enzyme participates in arginine and proline metabolism.
References
edit- Singh RM, Adams E (1965). "Enzymatic deamination of delta-1-pyrroline-4-hydroxy-2-carboxylate to 2,5-dioxovalerate (alpha-ketoglutaric semialdehyde)". The Journal of Biological Chemistry. 240 (11): 4344–51. PMID 5845838.
- Singh RM, Adams E (Nov 1965). "Isolation and identification of 2,5-dioxovalerate, an intermediate in the bacterial oxidation of hydroxyproline". The Journal of Biological Chemistry. 240 (11): 4352–6. PMID 5845839.
