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G5885

Sigma-Aldrich

Glucose-6-phosphate Dehydrogenase from Leuconostoc mesenteroides

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

Synonym(s):

G-6-P-DH

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bacterial (Leuconostoc mesenteroides)

Quality Level

type

Type XXIV

form

lyophilized powder

specific activity

>= 550 units/mg protein (biuret)

mol wt

128 kDa

composition

Protein, 15-40% biuret

application(s)

agriculture

foreign activity

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

storage temp.

2-8°C

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General description

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.

Application

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

Biochem/physiol Actions

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.

Unit Definition

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.

Physical form

Lyophilized powder containing Ficoll and Tris buffer salts

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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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
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
Hana A Dibe et al.
Physiological reports, 8(3), e14370-e14370 (2020-02-16)
The liver is the primary metabolic organ involved in the endogenous production of glucose through glycogenolysis and gluconeogenesis. Hepatic glucose production (HGP) is increased via neural-hormonal mechanisms such as increases in catecholamines. To date, the effects of prior exercise training
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)
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

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