Merck

G5885

Sigma-Aldrich

葡萄糖-6-磷酸脱氢酶 来源于肠系膜明串珠菌

lyophilized powder, >= 550 units/mg protein (biuret)

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别名:
G-6-P-DH
CAS号:
EC 号:
MDL编号:
NACRES:
NA.54

生物来源

bacterial (Leuconostoc mesenteroides)

质量水平

类型

Type XXIV

形式

lyophilized powder

specific activity

>= 550 units/mg protein (biuret)

分子量

128 kDa

组成

Protein, 15-40% biuret

application(s)

agriculture

异质活性

6-Phosphogluconic dehydrogenase, hexokinase, NADH oxidase and NADPH oxidase ≤0.005%
PGI ≤0.01%

储存温度

2-8°C

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此商品
G5760G8404G4134
specific activity

>= 550 units/mg protein (biuret)

specific activity

550-1,100 units/mg protein (biuret)

specific activity

≥550 units/mg protein (biuret)

specific activity

200-400 units/mg protein (modified Warburg-Christian)

mol wt

128 kDa

mol wt

54 kDa

mol wt

128 kDa

mol wt

128 kDa

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

Quality Level

300

Quality Level

200

Quality Level

300

Quality Level

200

foreign activity

6-Phosphogluconic dehydrogenase, hexokinase, NADH oxidase and NADPH oxidase ≤0.005%, PGI ≤0.01%

foreign activity

6-Phosphogluconic dehydrogenase, hexokinase, NADH oxidase and NADPH oxidase ≤0.005%, PGI ≤0.01%

foreign activity

creatine phosphokinase, glutathione reductase, myokinase, NADH oxidase, NADPH oxidase, phosphoglucomutase, 6-phosphogluconic dehydrogenase, phosphoglucose isomerase, lactic dehydrogenase, hexokinase ≤0.01%

foreign activity

-

一般描述

葡萄糖-6-磷酸脱氢酶(G-6-PDH)由His-Asp催化二联体构成,并以同二聚体形式存在。结构上,G-6-PDH在辅酶结合结构域内包含罗斯曼折叠构成的二核苷酸结合区域。还具有一个较大的β + α结构域,在374位有一个独特的天冬氨酸残基。

应用

来自肠膜明串珠菌的葡萄糖-6-磷酸脱氢酶已联用己糖激酶进行小鼠肝样品中的葡萄糖测定。

生化/生理作用

葡萄糖-6-磷酸脱氢酶(G-6-PDH)可使用烟酰胺腺嘌呤二核苷酸磷酸(NADP+)或NAD+作为辅酶,在细菌代谢中具有重要作用。
葡萄糖-6-磷酸脱氢酶(G6PD)催化葡萄糖-6-磷酸转化为6-磷酸葡糖酸内酯,作为磷酸戊糖途径的第一步。

单位定义

一个单元在NAD 存在下,在pH 7.8,30℃ 下,每分钟将 1.0 μmole的D-葡萄糖-6-磷酸氧化成 6-磷酸-D-葡萄糖酸盐。

外形

含有Ficoll和Tris 缓冲盐的冻干粉

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 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)


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V Vought et al.
Biochemistry, 39(49), 15012-15021 (2000-12-07)
The roles of particular amino acids in substrate and coenzyme binding and catalysis of glucose-6-phosphate dehydrogenase of Leuconostoc mesenteroides have been investigated by site-directed mutagenesis, kinetic analysis, and determination of binding constants. The enzyme from this species has functional dual
M S Cosgrove et al.
Biochemistry, 39(49), 15002-15011 (2000-12-07)
The role of Asp-177 in the His-Asp catalytic dyad of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides has been investigated by a structural and functional characterization of the D177N mutant enzyme. Its three-dimensional structure has been determined by X-ray cryocrystallography in
J Pozueta-Romero et al.
FEBS letters, 291(2), 233-237 (1991-10-21)
The standardized enzyme coupling method for assaying sucrose synthase activities in the direction of sucrose cleavage was reexamined using enzyme preparations from cultured cells of sycamore (Acer pseudoplatanus L.) and spinach leaves (Spinacea oleracea). Both ATP and Tris, commonly utilized
A simple ultramicro method for determination of pyridine nucleotides in tissues.
J S Nisselbaum et al.
Analytical biochemistry, 27(2), 212-217 (1969-02-01)
Sofia Garcia et al.
Human molecular genetics, 31(5), 692-704 (2021-09-25)
We analyzed early brain metabolic adaptations in response to mitochondrial dysfunction in a mouse model of mitochondrial encephalopathy with complex IV deficiency [neuron-specific COX10 knockout (KO)]. In this mouse model, the onset of the mitochondrial defect did not coincide with

实验方案

To measure glucose-6-phosphate dehydrogenase activity, beta-nicotinamide adenine dinucleotide phosphate is used in a spectrophotometric rate determination assay at 340 nm.

在测定6-磷酸葡萄糖脱氢酶活性时,使用β-烟酰胺腺嘌呤二核苷酸磷酸在340 nm处通过分光光度法进行测定。

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