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G6880

Sigma-Aldrich

α-Glycerophosphate Dehydrogenase from rabbit muscle

Type X, lyophilized powder, ≥100 units/mg protein

Synonym(s):

sn-Glycerol-3-phosphate Dehydrogenase from rabbit muscle, sn-Glycerol-3-phosphate:NAD+ 2-oxidoreductase

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About This Item

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

type

Type X

Quality Level

form

lyophilized powder

specific activity

≥100 units/mg protein

composition

Protein, ≥75%

foreign activity

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

shipped in

wet ice

storage temp.

−20°C

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Application

α-glycerophosphate dehydrogenase was used in 2-deoxy-ribose 5-phosphate aldolase (DERA) cleavage (retroaldol) assay.

Biochem/physiol Actions

α-glycerophosphate dehydrogenase catalyzes the conversion of dihydroxyacetone to glycerol phosphate.

Unit Definition

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

Physical form

Lyophilized sulfate-free powder containing buffer salts as citrate and EDTA

Analysis Note

Protein determined by biuret

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Grace DeSantis et al.
Bioorganic & medicinal chemistry, 11(1), 43-52 (2002-12-07)
2-Deoxyribose-5-phosphate aldolase (DERA, EC 4.1.2.4) catalyzes the reversible aldol reaction between acetaldehyde and D-glyceraldehyde-3-phosphate to generate D-2-deoxyribose-5-phosphate. It is unique among the aldolases as it catalyzes the reversible asymmetric aldol addition reaction of two aldehydes. In order to expand the
Feng Peng et al.
Yeast (Chichester, England), 27(2), 115-121 (2009-12-17)
In this study, a novel glycerol-3-phosphate dehydrogenase (NAD(+)) (EC1.1.1.8) gene (PfGPD) was cloned from halotolerant yeast Pichia farinosa, using degenerate reverse transcription (RT)-PCR and rapid amplification of cDNA ends (RACE) methods. The full-length cDNA of the PfGPD gene is 1403
Georg Hubmann et al.
Applied and environmental microbiology, 77(17), 5857-5867 (2011-07-05)
Gpd1 and Gpd2 are the two isoforms of glycerol 3-phosphate dehydrogenase (GPDH), which is the rate-controlling enzyme of glycerol formation in Saccharomyces cerevisiae. The two isoenzymes play crucial roles in osmoregulation and redox balancing. Past approaches to increase ethanol yield
Vishist K Jain et al.
Applied microbiology and biotechnology, 93(1), 131-141 (2011-07-02)
Saccharomyces cerevisiae maintains a redox balance under fermentative growth conditions by re-oxidizing NADH formed during glycolysis through ethanol formation. Excess NADH stimulates the synthesis of mainly glycerol, but also of other compounds. Here, we investigated the production of primary and
Chung-Cheng Kao et al.
Planta medica, 76(7), 694-696 (2009-11-26)
Green tea catechins, especially (-)-epigallocatechin-3-gallate (EGCG), are known to regulate obesity and fat accumulation. We performed a kinetic analysis in a cell-free system to determine the mode of inhibition of glycerol-3-phosphate dehydrogenase (GPDH; EC 1.1.1.8) by EGCG. GPDH catalyzes the

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