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G2253

Sigma-Aldrich

L-Glutamic acid γ-monohydroxamate

≥97% (TLC)

Synonyma:

L-γ-Glutamylhydroxamic acid, L-5-N-Hydroxyglutamine

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen


About This Item

Empirický vzorec (Hillův zápis):
C5H10N2O4
Číslo CAS:
Molekulová hmotnost:
162.14
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26

Název produktu

L-Glutamic acid γ-monohydroxamate,

assay

≥97% (TLC)

Quality Level

form

powder

color

white to off-white

application(s)

detection

storage temp.

−20°C

SMILES string

NC(CCC(=O)NO)C(O)=O

InChI

1S/C5H10N2O4/c6-3(5(9)10)1-2-4(8)7-11/h3,11H,1-2,6H2,(H,7,8)(H,9,10)

InChI key

YVGZXTQJQNXIAU-UHFFFAOYSA-N

Application

L-Glutamic acid γ-monohydroxamate has been used as a standard to calculate transglutaminase (TGase) activity.

Biochem/physiol Actions

L-Glutamic acid γ-monohydroxamate [L-Glu(gamma)HXM] is used as a vanadium ligand which potentiates vanadiums metabolic activity. L-Glu(gamma)HXM is also used as a substrate for E. coli asparagine synthetase B and as an ATP-dependent irreversible inhibitor of Escherichia coli gamma-glutamylcysteine synthetase.

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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Osvědčení o analýze (COA)

Lot/Batch Number

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Navštívit knihovnu dokumentů

M Katoh et al.
Bioscience, biotechnology, and biochemistry, 62(7), 1455-1457 (1998-08-28)
Incubation of Escherichia coli gamma-glutamylcysteine synthetase with L-glutamic acid gamma-monohydroxamate and ATP caused slow but irreversible inhibition of the enzyme, and more than 90% activity was lost in three days. The enzyme was not inactivated when ATP was absent or
N Seiler et al.
Neurochemical research, 15(3), 301-305 (1990-03-01)
The method for the assay of glutamine synthetase (GlnS) relies on the gamma-glutamyl transferase reaction, i.e. the formation of glutamyl-gamma-hydroxamate from glutamine and hydroxylamine, and the chromatographic separation of the reaction product from the reactants. The method is not only
Michael J Muhitch
Journal of plant physiology, 160(6), 601-605 (2003-07-23)
In maize (Zea mays L.), GSp1, the predominant GS isozyme of the developing kernel, is abundant in the pedicel and pericarp, but absent from the endosperm and embryo. Determinations of GSp1 tissue distribution in vegetative tissues have been limited thus
I Goldwaser et al.
Molecular pharmacology, 58(4), 738-746 (2000-09-22)
Several ligands, when complexed with vanadium, potentiate its insulinomimetic activity both in vivo and in vitro. We have recently found that L-Glu-gamma-monohydroxamate (HXM) and L-Asp(beta)HXM were especially potent in this regard. In the present study, we used vanadium-enriched adipose cells
Matteo Tegoni et al.
Dalton transactions (Cambridge, England : 2003), (9)(9), 1329-1333 (2004-07-15)
The equilibria of copper(II) with (S)-glutamic-gamma-hydroxamic acid (H2L) were investigated in aqueous solution by different techniques: glass electrode potentiometry; calorimetry; VIS and CD spectrophotometry; and ES-MS. An unexpected pentacopper(II) 12-metallacrown-4 [Cu5L4H(-4)](2-) was detected, analogous to those well known formed by

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