Gamma-glutamyl-gamma-aminobutyrate hydrolase
| Gamma-glutamyl-gamma-aminobutyrate hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.94 | ||||||||
| 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 gamma-glutamyl-gamma-aminobutyrate hydrolase (EC 3.5.1.94) is an enzyme that catalyzes the chemical reaction
- 4-(gamma-glutamylamino)butanoate + H2O 4-aminobutanoate + L-glutamate
Thus, the two substrates of this enzyme are 4-(gamma-glutamylamino)butanoate and H2O, whereas its two products are 4-aminobutanoate and L-glutamate.
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 4-(gamma-glutamylamino)butanoate amidohydrolase. Other names in common use include gamma-glutamyl-GABA hydrolase, PuuD, and YcjL. This enzyme participates in urea cycle and metabolism of amino groups.
References
[edit]- Kurihara S, Oda S, Kato K, Kim HG, Koyanagi T, Kumagai H, Suzuki H (2005). "A novel putrescine utilization pathway involves gamma-glutamylated intermediates of Escherichia coli K-12". J. Biol. Chem. 280 (6): 4602–8. doi:10.1074/jbc.M411114200. PMID 15590624.
