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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:
9001-40-5
Enzyme Commission number:
1.1.1.49 (BRENDA, IUBMB)
EC Number:
232-602-6
MDL number:
MFCD00081656
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bacterial (Leuconostoc mesenteroides)

Quality Level

300

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
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

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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
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
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
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Protocols

Enzymatic Assay of Glucose-6-Phosphate Dehydrogenase (EC 1.1.1.49)

Enzymatic Assay of Glucose-6-Phosphate Dehydrogenase (EC 1.1.1.49)

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