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Merck
CN

79854

Alcohol Dehydrogenase equine

recombinant, expressed in E. coli, ≥10.0 U/mL

Synonym(s):

ADH

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About This Item

CAS Number:
UNSPSC Code:
12352204
EC Number:
232-870-4
MDL number:
EC Number:
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recombinant

expressed in E. coli

form

liquid

specific activity

≥10.0 U/mL

storage temp.

−20°C

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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 sit for the alcohol substrate.

Other Notes

1 U corresponds to the amount of enzyme which reduces 1 μmol benzaldehyde per minute at pH 7.0 and 30°C.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

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Jong Ho Park et al.
Bioscience, biotechnology, and biochemistry, 76(12), 2294-2300 (2012-12-12)
Here, the impact of an extract derived from green tea (Camellia sinensis) and fermentation with Lactobacilli fermentum strain OCS19 was explored with acute alcohol-induced liver damage. The study employed the HepG2 hepatic cell line and an in vivo murine model
Yoshiyuki Kimura et al.
Fitoterapia, 84, 163-169 (2012-11-20)
The Curcuma zedoaria rhizome has been used traditionally to treat gastrointestinal diseases as an aromatic stomachic drug, and this is currently used to treat alcohol-induced loss of appetite and nausea in Japan. We examined the effects of various fractions and
N L Vekshin
Biofizika, 57(5), 741-745 (2012-11-10)
The dynamics of proteins, detected by fluorescence, consists of three components: spontaneous dynamics, dipole-dipole photo-induced dynamics, thermal photo-induced dynamics. The photo-induced dynamics can lead to activation as well as inactivation of enzymes.
Chien-Ping Chiang et al.
Alcoholism, clinical and experimental research, 36(12), 2047-2058 (2012-12-13)
Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) are principal enzymes responsible for metabolism of ethanol (EtOH). Functional polymorphisms of ADH1B, ADH1C, and ALDH2 genes occur among racial populations. This study aimed to systematically determine the functional expressions and cellular localization
Diya Alsafadi et al.
Extremophiles : life under extreme conditions, 17(1), 115-122 (2012-11-28)
The effect of various organic solvents on the catalytic activity, stability and substrate specificity of alchohol dehydrogenase from Haloferax volcanii (HvADH2) was evaluated. The HvADH2 showed remarkable stability and catalysed the reaction in aqueous-organic medium containing dimethyl sulfoxide (DMSO) and

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