G9270
γ-Glutamyltranspeptidase from equine kidney
Type VI, 5-12 units/mg solid
Synonym(s):
γ-GT, γ-Glutamyltransferase, (5-Glutamyl)peptide:amino-acid 5-glutamyltransferase, GGTP
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-931-5
MDL number:
Specific activity:
5-12 units/mg solid
Biological source:
equine kidney
biological source
equine kidney
Quality Level
type
Type VI
form
solid
specific activity
5-12 units/mg solid
storage temp.
−20°C
General description
Gamma-Glutamyltranspeptidase is a heterodimeric enzyme and belongs to the superfamily of N-terminal nucleophile hydrolases.
Application
Gamma-glutamyltranspeptidase from equine kidney has been used:
- to identify the formation of 4-S-Cysteinyltetrodotoxin in the liver of Fugu pardalis
- as a standard to determine the activity of gamma-glutamyltransferase from human B-cell lymphoma cell lysates
- to hydrolyze isopeptides to study its effects on tubulin aggregation
Biochem/physiol Actions
Gamma-Glutamyltranspeptidase participates in glutathione metabolism and it catalyzes the cleavage of gamma-glutamyl compounds, such as glutathione. It also plays a role in the transfer of gamma-glutamyl moiety to amino acids and peptides.
Analysis Note
Crude
Other Notes
One unit will liberate 1.0 μmole of p-nitroaniline from L-γ-glutamyl-p-nitroanilide per min at pH 8.5 at 25°C.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Lawrence M Schopfer et al.
The Journal of biological chemistry, 293(35), 13566-13577 (2018-07-15)
Exposure to organophosphorus toxicants (OP) can have chronic adverse effects that are not explained by inhibition of acetylcholinesterase, the cause of acute OP toxicity. We therefore hypothesized that OP-induced chronic illness is initiated by the formation of organophosphorus adducts on
Gina Boanca et al.
The Journal of biological chemistry, 281(28), 19029-19037 (2006-05-05)
Gamma-glutamyltranspeptidase (gammaGT), a member of the N-terminal nucleophile hydrolase superfamily, initiates extracellular glutathione reclamation by cleaving the gamma-glutamyl amide bond of the tripeptide. This protein is translated as an inactive proenzyme that undergoes autoprocessing to become an active enzyme. The
Mari Yotsu-Yamashita et al.
Chemical research in toxicology, 18(5), 865-871 (2005-05-17)
The metabolic pathway of tetrodotoxin (TTX), a powerful and specific voltage-gated sodium channel blocker, has not been well-clarified either in TTX-poisoned patients or in puffer fish. 4-S-CysteinylTTX (4-CysTTX) was isolated from the liver of the puffer fish, Fugu pardalis, as