Biology:Gamma-glutamyl-gamma-aminobutyrate hydrolase
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Gamma-glutamyl-gamma-aminobutyrate hydrolase | |||||||||
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Identifiers | |||||||||
EC number | 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 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
- "A novel putrescine utilization pathway involves gamma-glutamylated intermediates of Escherichia coli K-12". J. Biol. Chem. 280 (6): 4602–8. 2005. doi:10.1074/jbc.M411114200. PMID 15590624.
Original source: https://en.wikipedia.org/wiki/Gamma-glutamyl-gamma-aminobutyrate hydrolase.
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