Accéder au contenu
Merck

G5760

Glucose-6-phosphate Dehydrogenase from Leuconostoc mesenteroides

Type XXIII, ammonium sulfate suspension, 550-1,100 units/mg protein (biuret), ≥2.0 mg/mL Biuret

Synonyme(s) :

G-6-P-DH

Se connecter pour consulter les tarifs organisationnels et contractuels.

Sélectionner une taille de conditionnement

Changer de vue

A propos de cet article

Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-602-6
MDL number:
Numéro CE :
eCl@ss:
32160703
Specific activity:
550-1,100 units/mg protein (biuret)
Biological source:
bacterial (Leuconostoc mesenteroides)
Concentration:
≥2.0 mg/mL Biuret
Service technique
Besoin d'aide ? Notre équipe de scientifiques expérimentés est là pour vous.
Laissez-nous vous aider


biological source

bacterial (Leuconostoc mesenteroides)

Quality Segment

type

Type XXIII

form

ammonium sulfate suspension

specific activity

550-1,100 units/mg protein (biuret)

mol wt

54 kDa

concentration

≥2.0 mg/mL Biuret

foreign activity

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

storage temp.

2-8°C

General description

Research area: Cell Signaling

Glucose-6-phosphate dehydrogenase (G6PD) is found in the cytoplasm of all cells. The G6PD enzyme is encoded by the Gd gene, located on the long arm of the X chromosome.Glucose-6-phosphate Dehydrogenase (G6PD) from Leuconostoc mesenteroides catalyzes the oxidation of glucose 6-phosphate in the presence of nicotinamide adenine dinucleotide (NAD+) or nicotinamide adenine dinucleotide phosphate (NADP+). It corresponds to a molecular weight of 54 kDa and exists as a homodimer.

Application

Glucose-6-phosphate Dehydrogenase from Leuconostoc mesenteroides has been used:

  • as a component of reaction mixture for assaying mannose- and glucose-6-phosphate activity
  • as a component of reaction mixture in the nevirapine inhibition studies in human hepatic microsomes
  • in the glucose-phosphorylating activity of chloroplast extracts
  • as a model to test the effect of seed protein fractions on enzyme protection during dehydration.
  • in assays for nicotinamide adenine dinucleotide and tissue pyridine nucleotides.

Biochem/physiol Actions

Glucose-6-phosphate dehydrogenase (G6PD) is a housekeeping enzyme that protects cells from damage caused by reactive oxygen species by supplying substrates that help prevent oxidative harm. G6PD from Leuconostoc mesenteroides catalyzes the oxidation of glucose 6-phosphate in the presence of nicotinamide adenine dinucleotide (NAD+) or nicotinamide adenine dinucleotide phosphate (NADP+) as the first step in the pentose phosphate pathway. Lysine 21 in the Glucose-6-phosphate Dehydrogenase (G6PD) is crucial for binding NAD+. G6PD uses NAD+ or NADP+ based on the catabolic or anabolic metabolic pathway.G6PD deficiency can lead to acute hemolysis, neonatal jaundice, or severe chronic non-spherocytic hemolytic anemia.
Glucose-6-phosphate dehydrogenase (G6PD) catalyzes the conversion of glucose-6-phosphate to 6-phosphogluconolacetone as the first step in the pentose phosphate pathway.

Physical form

Suspension in 2.7 M (NH4)2SO4 solution containing 42 mM Tris and 0.8 mM MgCl2

Other Notes

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.


Still not finding the right product?


Pictogrammes

Health hazard

Mot-clé

Danger

Codes de danger

Mentions de précaution

Hazard Classifications

Resp. Sens. 1

Classe de stockage

11 - Combustible Solids

WGK

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

EPI (équipement de protection individuelle)

Eyeshields, Gloves, type N95 (US)



Faites votre choix parmi les versions les plus récentes :

Certificats d'analyse (COA)

Lot/Batch Number

Vous ne trouvez pas la bonne version ?

Si vous avez besoin d'une version particulière, vous pouvez rechercher un certificat spécifique par le numéro de lot.

Déjà en possession de ce produit ?

Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents