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
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biological source
equine kidney
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.
Quality
Crude
Unit Definition
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.
inhibitor
Product No.
Description
Pricing
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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
Karin Bracht et al.
Journal of cancer research and clinical oncology, 133(12), 957-967 (2007-06-15)
The aim of this study was to characterize three new, recently established non-Hodgkin lymphoma cell lines (GUMBUS, DOGUM, and DOGKIT), isolated from patients developing high-clinical resistance to cytotoxic therapy, with respect to sensitivity toward 21 antitumor drugs from different classes
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
H Suzuki et al.
Amino acids, 32(3), 333-340 (2006-10-13)
Some amino acids and peptides, which have low solubility in water, become much more soluble following gamma-glutamylation. Compounds become more stable in the blood stream with gamma-glutamylation. Several gamma-glutamyl compounds are known to have favorable physiological effects on mammals. Gamma-glutamylation
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