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Key Documents

G5885

Sigma-Aldrich

Glucose-6-phosphate Dehydrogenase from Leuconostoc mesenteroides

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

Synonyme(s) :

G-6-P-DH

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

bacterial (Leuconostoc mesenteroides)

Niveau de qualité

Type

Type XXIV

Forme

lyophilized powder

Activité spécifique

>= 550 units/mg protein (biuret)

Poids mol.

128 kDa

Composition

Protein, 15-40% biuret

Application(s)

agriculture

Activité étrangère

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

Température de stockage

2-8°C

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Description générale

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.

Actions biochimiques/physiologiques

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.

Définition de l'unité

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.

Forme physique

Lyophilized powder containing Ficoll and Tris buffer salts

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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

Protocoles

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

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