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About This Item
Empirical Formula (Hill Notation):
C5H10N2O4
CAS Number:
Molecular Weight:
162.14
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26
MDL number:
Product Name
L-Glutamic acid γ-monohydroxamate,
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
assay
≥97% (TLC)
form
powder
color
white to off-white
application(s)
detection
storage temp.
−20°C
Quality Level
Related Categories
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
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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
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
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
Yibin Xu et al.
Protein expression and purification, 34(1), 142-146 (2004-02-10)
A soluble N-terminal domain of the Escherichia coli adenylyl transferase (ATase) is responsible for deadenylylation activity of the intact enzyme. Previous studies of the deadenylylation activity have involved a fragment, AT-N423 (residues 1 to 423), which was extended by 17
Changes in enzymatic activity of fish and slaughter animals meat after high pressure treatment at subzero temperatures
Malinowska-Panczyk E and Kolodziejska I
Polish Journal of Food and Nutrition Sciences, 68(2), 125-131 (2018)
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