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G1135

Sigma-Aldrich

L-Glutamic acid γ-(4-nitroanilide)

γ-glutamyl transpeptidase substrate

Synonym(s):

L-γ-Glutamyl-p-nitroanilide, L-Glutamic acid 5-(4-nitroanilide)

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About This Item

Linear Formula:
C11H13N3O5
CAS Number:
7300-59-6
Molecular Weight:
285.25
Beilstein:
2818758
EC Number:
230-748-5
MDL number:
MFCD00036218
UNSPSC Code:
12352204
PubChem Substance ID:
24895042
NACRES:
NA.83

Assay

≥98% (HPLC)

form

powder

solubility

formic acid: 50 mg/mL, clear to slightly hazy

storage temp.

2-8°C

SMILES string

N[C@@H](CCC(=O)Nc1ccc(cc1)[N+]([O-])=O)C(O)=O

InChI

1S/C11H13N3O5/c12-9(11(16)17)5-6-10(15)13-7-1-3-8(4-2-7)14(18)19/h1-4,9H,5-6,12H2,(H,13,15)(H,16,17)/t9-/m0/s1

InChI key

WMZTYIRRBCGARG-VIFPVBQESA-N

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Substrates

Substrate for γ-glutamyl transpeptidase

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

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L Dvoráková et al.
General physiology and biophysics, 15(5), 403-413 (1996-10-01)
The initial rate kinetics of rat kidney gamma-glutamyl transpeptidase were measured using L-gamma-glutamyl-p-nitroanilide and glycyl-glycine as the donor and the acceptor substrate, respectively. Experimental data were fitted with the initial rate equation, and the obtained results indicated that: (1) Michaelis
Gololobov MYu et al.
The Biochemical journal, 304 ( Pt 3), 869-876 (1994-12-15)
Acyl-transfer catalysed by gamma-glutamyltranspeptidase from bovine kidney was studied using gamma-L- and gamma-D-Glu-p-nitroanilide as the donor and GlyGly as the acceptor. The transfer of the gamma-Glu group to GlyGly was shown to be accompanied by transfer of the gamma-Glu group
L Chu et al.
Oral microbiology and immunology, 24(3), 236-242 (2009-05-07)
Our previous studies demonstrated that three enzymes, gamma-glutamyltransferase (GGT), cysteinylglycinase (CGase) and cystalysin, are required for the catabolism of glutathione to produce hydrogen sulfide (H(2)S) in Treponema denticola. In this study, we examined glutathione catabolism in Aggregatibacter actinomycetemcomitans. The GGT
Y Ikeda et al.
Journal of biochemistry, 119(6), 1166-1170 (1996-06-01)
gamma-Glutamyl transpeptidase possesses two histidine residues at positions 383 and 505 which are conserved in all mammalian and bacterial species. In order to elucidate the functions of these residues, we prepared mutants in which these residues were replaced by Ala.
K Abe et al.
Bioscience, biotechnology, and biochemistry, 61(10), 1621-1625 (1997-11-15)
Two isozymes of gamma-glutamyltranspeptidase, GGT-A and GGT-B, were purified to electrophoretic homogeneity from a culture broth of Bacillus subtilis TAM-4, which produces poly(gamma-glutamic acid) (PGA) de novo. GGT-A was composed of three subunits with molecular weights of 23,000 (I), 39,000
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