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G6751

Sigma-Aldrich

α-Glycerophosphat-Dehydrogenase aus Kaninchenmuskel

Type I, ammonium sulfate suspension, 100-300 units/mg protein

Synonym(e):

sn-Glycerol-3-phosphate Dehydrogenase

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About This Item

CAS-Nummer:
9075-65-4
EC-Nummer:
1.1.1.8 (BRENDA, IUBMB)
EG-Nummer:
232-982-3
MDL-Nummer:
MFCD00130487
UNSPSC-Code:
12352204
NACRES:
NA.54

Biologische Quelle

rabbit muscle

Qualitätsniveau

200

Typ

Type I

Form

ammonium sulfate suspension

Spezifische Aktivität

100-300 units/mg protein

Lagerbedingungen

(Tightly closed)

Methode(n)

activity assay: suitable

Farbe

white

Fremdaktivität

Lactic dehydrogenase, pyruvate kinase, aldolase, and glyceraldehyde-3-phosphate dehydrogenase ≤0.01%
Triosephosphate isomerase ≤0.02%

Lagertemp.

2-8°C

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Allgemeine Beschreibung

α-Glycerophosphate dehydrogenase is a membrane protein and a flavin-linked primary dehydrogenase.

Research area: Cell Signaling

Anwendung

α-Glycerophosphate Dehydrogenase from rabbit muscle has been used:
  • in the reaction mixture to measure the glycerol kinase activity
  • to demonstrate compartmentalized enzymatic reactions where NADH is involved
  • in the reaction mixture assay for L-fuculose-1-phosphate aldolase

Biochem./physiol. Wirkung

α-Glycerophosphate dehydrogenase catalyzes the oxidation of L-α-glycerophosphate (Glp) to form dihydroxyacetone phosphate (DHAP) and hydrogen peroxide (H2O2). This enzyme is associated with respiratory electron transport chain, glycolysis, and phospholipid metabolism.

Einheitendefinition

One unit will convert 1.0 μmole of dihydroxyacetone phosphate to α-glycerophosphate per min at pH 7.4 at 25 °C.

Physikalische Form

Crystalline suspension in 3.2 M (NH4)2SO4 and 0.1 g/L EDTA solution, pH 6.0

Angaben zur Herstellung

Prepared by modification of the method of Fondy.

Hinweis zur Analyse

Protein determined by biuret.

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Piktogramme

Health hazard
GHS08

Signalwort

Danger

H-Sätze

H334

Gefahreneinstufungen

Resp. Sens. 1

Lagerklassenschlüssel

12 - Non Combustible Liquids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

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Structural studies on nicotinamide adenine dinucleotide-linked L-glycerol 3-phosphate dehydrogenase crystallized from rat skeletal muscle.
T P Fondy et al.
The Journal of biological chemistry, 243(11), 3148-3160 (1968-06-10)
Somchart Maenpuen et al.
The FEBS journal, 282(16), 3043-3059 (2015-02-26)
L-α-glycerophosphate oxidase is an FAD-dependent enzyme that catalyzes the oxidation of L-α-glycerophosphate (Glp) by molecular oxygen to generate dihydroxyacetone phosphate (DHAP) and hydrogen peroxide (H2O2). The catalytic properties of recombinant His6-GlpO from Mycoplasma pneumoniae (His6-MpGlpO) were investigated through transient and
Joanne I Yeh et al.
Proceedings of the National Academy of Sciences of the United States of America, 105(9), 3280-3285 (2008-02-26)
Sn-glycerol-3-phosphate dehydrogenase (GlpD) is an essential membrane enzyme, functioning at the central junction of respiration, glycolysis, and phospholipid biosynthesis. Its critical role is indicated by the multitiered regulatory mechanisms that stringently controls its expression and function. Once expressed, GlpD activity
Optimal conditions for biomass and recombinant glycerol kinase production using the yeast Pichia pastoris
Aizemberg R, et al.
Food Technology and Biotechnology, 49(3), 329-329 (2011)
Tiia Kittilä et al.
Chembiochem : a European journal of chemical biology, 17(7), 576-584 (2016-01-12)
Nonribosomal peptide synthetases (NRPSs) produce many important and structurally complex natural products. Because of their architectures, reprogramming NRPSs has long been attempted to access new bioactive compounds. However, detailed characterization of NRPS catalysis and substrate selectivity by adenylation (A) domains
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