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G9270

Sigma-Aldrich

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:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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
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
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

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