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Merck

G6880

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:
9075-65-4
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-982-3
MDL number:
MFCD00040474
EC Number:
1.1.1.8 (BRENDA, IUBMB)
Specific activity:
≥100 units/mg protein

Key Documents

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type

Type X

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

Quality Level

200

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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.

Physical form

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

Analysis Note

Protein determined by biuret

Other Notes

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

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
0000500813
0000500813
0000483752
0000483752
0000429784

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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
Kyung Ok Yu et al.
Journal of biotechnology, 150(2), 209-214 (2010-09-22)
Ethanol plays an important role in substituting the increasingly limited oil as the high-value, renewable fuel. In our previous studies, we successfully established the conversion of glycerol to ethanol by overexpression of pGcyaDak with pGup1Cas in Saccharomyces cerevisiae. In addition
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
Zhong-peng Guo et al.
Metabolic engineering, 13(1), 49-59 (2010-12-04)
To synthesize glycerol, a major by-product during anaerobic production of ethanol, the yeast Saccharomyces cerevisiae would consume up to 4% of the sugar feedstock in typical industrial ethanol processes. The present study was dedicated to decreasing the glycerol production mostly
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
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