Identification | Back Directory | [Name]
EC 1.1.1.2 | [CAS]
9028-12-0 | [Synonyms]
TBADH EC 1.1.1.2 KETOREDUCTASE T KETOREDUCTASE LB frommicrobialsource KETOREDUCTASE CDX003 AlcoholdehydrogenaseM Alcohol dehydrogenases ALCOHOL DEHYDROGENASE T ALCOHOL DEHYDROGENASE LB alcohol dehydrogenase,ADH Alcohol Dehydrogenase 005 Ketoreductase, Recombinant ALCOHOL DEHYDROGENASE CDX003 ALCOHOL: NADP+ OXIDOREDUCTASE NADPH Dependent Ketoreductase ALCOHOL DEHYDROGENASE, >0.4 U/MG* Alcohol Dehydrogenase, recombinant ADH, Alcohol:NADP+ oxidoreductase Alcohol:NADP+ oxidoreductase, TBADH ALCOHOL DEHYDROGENASE, NADP+ DEPENDENT ALCOHOL DEHYDROGENASE FROM THERMOANAERO& NADPH Dependent Primary Alcohol Dehydrogenases alcohol dehydrogenase from lactobacillus kefir Alcohol Dehydrogenase from Candida boidinii ALCOHOL DEHYDROGENASE (THERMOANAEROBIUM BROCKII) NADPH Dependent Ketoreductase Custom Screening Kit NADPH Dependent Ketoreductase Single Screening Kit NADP-LINKED ALCOHOL-ALDEHYDE/KETONE OXIDOREDUCTASE ALCOHOL DEHYDROGENASE, NADP+ DEPENDENTFR OM THERMOA (S)-AROMATIC ALCOHOL DEHYDROGENASE, NADP+ DEPENDENT Alcohol Dehydrogenase, recombinant from E. coli
ALCOHOL DEHYDROGENASE FROM LACTOBACILLUS KEFIR, ~0.4 U/MG NADPH Dependent Primary Alcohol Dehydrogenases Screening Kit Alcohol Dehydrogenase (NADP+ dependent) from E. coli, Recombinant alcohol dehydrogenase, nadp+ dependent from thermoanaerobium brockii Dehydrogenase, alcohol (nicotinamide adenine dinucleotide phosphate) Native Thermoanaerobium brockii Alcohol Dehydrogenase, NADP+ dependent (S)-OXYNITRILASE FROM MANIHOT ESCULENTA (MANIOK, RECOMBINANT IN E. COLI) Native Thermoanaerobium sp. Aromatic Alcohol Dehydrogenase, NADP+ dependent (R)-Aromatic alcohol dehydrogenase, NADP+ dependent from Lactobacillus kefir (s)-aromatic alcohol dehydrogenase, nadp+ dependent from thermoanaerobium sp. Alcohol Dehydrogenase from Lactobacillus kefir,ADH, Alcohol:NADP+ oxidoreductase | [EINECS(EC#)]
232-823-8 | [MDL Number]
MFCD00130451 |
Chemical Properties | Back Directory | [storage temp. ]
−20°C
| [solubility ]
50 mM phosphate buffer pH 7.0: 1mg/mL, clear to faintly turbid, slightly yellow to deep brownish-yellow | [form ]
powder
| [color ]
white
| [Specific Activity]
5.0-15.0U/mg |
Hazard Information | Back Directory | [Uses]
Component of NADH recycling systems. Substrate specificity limited to low molecular weight alcohols. | [General Description]
Alcohol:NAD+ oxidoreductase. Alcohol dehydrogenase (ADH) from yeast is a metalloenzyme containing four zinc atoms per molecule. NAD+ is its coenzyme. | [Biochem/physiol Actions]
Alcohol dehydrogenase catalyzes the oxidative conversion of alcohol into aldehyde. It has a homodimeric structure with a co-enzyme binding domain at the C-terminal and an N-terminal catalytic domain. The active site is located at the interdomain cleft. Binding of NAD+ in the active site causes conformational changes which create the binding site for the alcohol substrate. |
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Creative Enzymes
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SIGMA-RBI
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Nagase Group
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