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Merck
CN

G1270

L-谷氨酰胺合成酶 来源于大肠杆菌

lyophilized powder, 400-2,000 units/mg protein

别名:

L-Glutamate:ammonia ligase (ADP-forming)

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化学文摘社编号:
MDL编号:
UNSPSC代码:
12352204
NACRES:
NA.26
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表单

lyophilized powder

质量水平

比活

400-2,000 units/mg protein

纯化方式

affinity chromatography

包含

dithioerythritol as preservative

组成

Protein, ~5% Lowry

溶解性

H2O: soluble 0.95-1.05 mg/mL, clear to hazy

UniProt登记号

异质活性

ATPase <0.2%

储存温度

−20°C

基因信息

Escherichia coli K12 ... glnA(948370)

一般描述

L-Glutamine Synthetase from bacteria shows dodecameric structure comprising of 12 active sites. Each active site termed bifunnel, has an ATP and glutamate binding sites. The dodecamer is stabilized by two hexameric rings.

应用

L-Glutamine Synthetase from Escherichia coli has been used in the synthesis of methylglutamine from methylammonium in E coli and in the glutamine synthetase protection activity of human thioredoxin peroxidase enzyme, AOE372.
L-Glutamine synthetase may be used for the purification of proteases from Escherichia coli.

生化/生理作用

谷氨酸降解酶
L-glutamine synthetase catalyzes the condensation of L-glutamate and ammonia to L-glutamine. It is a degradative enzyme for glutamic acid.
Nitrogen starvation dictates the expression of the glutamine synthetase (GS) gene in E. coli. GS plays a key role in ammonia assimilation in bacteria. Adenylylation of GS is catalyzed by adenylyltransferase. Adenylylation of GS modulates its catalytic functionality resulting in glutamine limitation in E coli.

外形

Contains potassium phosphate, sodium citrate and magnesium acetate buffer salts

其他说明

One unit will convert 1.0 μmole of L-glutamate to L-glutamine in 15 min at pH 7.1 at 37 °C.

象形图

Health hazard

警示用语:

Danger

危险声明

预防措施声明

危险分类

Resp. Sens. 1

储存分类代码

11 - Combustible Solids

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)

法规信息

常规特殊物品
此项目有

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation
Jin DY, et al.
The Journal of Biological Chemistry, 272(49), 30952-30961 (1997)
Reversible Adenylylation of Glutamine Synthetase Is Dynamically Counterbalanced during Steady-State
Okano H, et al.
Journal of molecular biology, 404(1), 522-536 (2010)
Huijuan Jia et al.
Molecular nutrition & food research, 57(2), 291-306 (2012-11-21)
This study addresses the effects of branched-chain amino acids (BCAA) on global gene expression in liver and skeletal muscle and the molecular mechanisms underlying the improvement in liver cirrhosis using DNA microarray analysis combined with RNase protection assay. Male Wistar
Peng Jiang et al.
Biochemistry, 51(45), 9032-9044 (2012-10-24)
Uridylyltransferase/uridylyl-removing enzyme (UTase/UR) catalyzes uridylylation of PII and deuridylylation of PII-UMP, with both activities regulated by glutamine. In a reconstituted UTase/UR-PII cycle containing wild-type UTase/UR, the steady-state modification of PII varied from nearly complete modification to nearly complete demodification as
Jane E Ladner et al.
Biochemistry, 51(51), 10121-10123 (2012-12-14)
The structure of PA5508 from Pseudomonas aeruginosa, a glutamine synthetase (GS) homologue, has been determined at 2.5 Å. Surprisingly, PA5508 forms single hexameric rings rather than the stacked double rings that are characteristic of GS. The C-terminal helical thong motif

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