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Merck
모든 사진(1)

주요 문서

G5885

Sigma-Aldrich

Glucose-6-phosphate Dehydrogenase from Leuconostoc mesenteroides

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

동의어(들):

G-6-P-DH

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About This Item

CAS Number:
효소 위원회 번호:
EC Number:
MDL number:
UNSPSC 코드:
12352204
NACRES:
NA.54

생물학적 소스

bacterial (Leuconostoc mesenteroides)

Quality Level

유형

Type XXIV

양식

lyophilized powder

특이 활성도

>= 550 units/mg protein (biuret)

분자량

128 kDa

구성

Protein, 15-40% biuret

응용 분야

agriculture

외래 활성

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

저장 온도

2-8°C

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일반 설명

Glucose-6-Phophate Dehydrogenase (G-6-PDH) comprises His-Asp catalytic dyad and exists as a homodimer. Structurally, G-6-PDH encompasses a Rossmann dinucleotide binding fold in the coenzyme binding domain region. It also harbors a large β + α domain and has a unique aspartate residue at position 374.

애플리케이션

Glucose-6-phosphate Dehydrogenase from Leuconostoc mesenteroides has been used along with hexokinase in the determination of glucose from mice liver samples.

생화학적/생리학적 작용

Glucose-6-Phophate Dehydrogenase (G-6-PDH) can utilize either nicotinamide adenine dinucleotide phosphate (NADP+) or NAD+ as coenzyme making it crucial for bacterial metabolism.
Glucose-6-phosphate dehydrogenase (G6PD) catalyzes the conversion of glucose-6-phosphate to 6-phosphogluconolacetone as the first step in the pentose phosphate pathway.

단위 정의

One unit will oxidize 1.0 μmole of D-glucose 6-phosphate to 6-phospho-D-gluconate per min in the presence of NAD at pH 7.8 at 30 °C.

물리적 형태

Lyophilized powder containing Ficoll and Tris buffer salts

픽토그램

Health hazard

신호어

Danger

유해 및 위험 성명서

예방조치 성명서

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

Eyeshields, Gloves, type N95 (US)


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문서 라이브러리 방문

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
Enzyme-stabilizing activity of seed trypsin inhibitors during desiccation
Ji-Ming Lam, Keng-Hock Pwee, Wendell Q. Sun, Yii-Leng Chua, Xing-Jun Wang
Plant Science, 142, 209-218 (1999)
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)

프로토콜

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

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