推荐产品
产品名称
L-谷氨酸& # 947;-单羟基己酸酯,
方案
≥97% (TLC)
质量水平
表单
powder
颜色
white to off-white
应用
detection
储存温度
−20°C
SMILES字符串
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
相关类别
应用
左旋谷氨酸γ-单异羟肟酸已用作计算谷氨酰胺转胺酶(TGase)活性的标准品。
生化/生理作用
L-谷氨酸& # 947;-单羟基肟酸盐[L-谷氨酸(γ)HXM]用作钒配体,增强钒代谢活性。L-Glu(γ)HXM也用作大肠杆菌 大肠杆菌天冬酰胺合成酶B的底物和作为ATP依赖性的大肠杆菌γ-谷氨酰半胱氨酸合成酶的不可逆抑制剂。
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
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
X Huang et al.
The Journal of biological chemistry, 275(34), 26233-26240 (2000-08-22)
The x-ray crystal structure of the heterodimeric carbamoyl phosphate synthetase from Escherichia coli has identified an intermolecular tunnel that connects the glutamine binding site within the small amidotransferase subunit to the two phosphorylation sites within the large synthetase subunit. The
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
Inhibition of malate-aspartate shuttle by the antitumor drug L-glutamic acid gamma-monohydroxamate in L1210 leukemia cells.
N Thomasset et al.
International journal of cancer, 51(2), 329-332 (1992-05-08)
S K Boehlein et al.
Biochemistry, 35(9), 3031-3037 (1996-03-05)
Escherichia coli asparagine synthetase B (AS-B) catalyzes the synthesis of asparagine from aspartic acid and glutamine in an ATP-dependent reaction. The ability of this enzyme to employ hydroxylamine and L-glutamic acid gamma-monohydroxamate (LGH) as alternative substrates in place of ammonia
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