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Key Documents

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G1135

Sigma-Aldrich

L-Glutamic acid γ-(4-nitroanilide)

γ-glutamyl transpeptidase substrate

Sinónimos:

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

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About This Item

Fórmula lineal:
C11H13N3O5
Número de CAS:
7300-59-6
Peso molecular:
285.25
Beilstein/REAXYS Number:
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

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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The reaction of oxidized and reduced glutathione (with some amino-acids) and L-gamma-glutamyl p-nitroanilide with sheep kidney tissue homogenate. An examination of the reaction products by paper chromatography.
P C Nicholas et al.
Biochemical Society transactions, 19(1), 50S-50S (1991-02-01)
Long-Liu Lin et al.
Applied microbiology and biotechnology, 73(1), 103-112 (2006-07-20)
A truncated gene from Bacillus lichenifromis ATCC 27811 encoding a recombinant gamma-glutamyltranspeptidase (BLrGGT) was cloned into pQE-30 to generate pQE-BLGGT, and the overexpressed enzyme was purified from the crude extract of IPTG-induced E. coli M15 (pQE-BLGGT) to homogeneity by nickel-chelate
M Moriguchi et al.
Archives of microbiology, 144(1), 15-19 (1986-02-01)
Three gamma-glutamyltranspeptidase (enzymes I, II and III) were partially purified from the cell free extracts of the cultured mycelia of Morchella esculenta Fr. The molecular masses of enzymes were 155,000 (I), 219,000 (II) and 102,000 (III). All of them catalyzed
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
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