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.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
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Nathan C Contino et al.
Journal of the American Society for Mass Spectrometry, 24(1), 101-108 (2012-12-01)
Charge detection mass spectrometry (CDMS) measurements have been performed for cytochrome c and alcohol dehydrogenase (ADH) monomer using a modified cone trap incorporating a cryogenically cooled JFET. Cooling the JFET increases its transconductance and lowers thermal noise, improving the signal
Shuo Zhou et al.
Biotechnology letters, 35(3), 359-365 (2012-11-20)
The gene encoding a novel short-chain alcohol dehydrogenase in the thermophilic bacterium, Carboxydothermus hydrogenoformans, was identified and overexpressed in Escherichia coli. The enzyme was thermally stable and displayed the highest activity at 70 °C and pH 6.0. It preferred NAD(H) over
Xingxing Diao et al.
Drug metabolism and disposition: the biological fate of chemicals, 41(2), 430-444 (2012-11-22)
3-n-Butylphthalide (NBP) is a cardiovascular drug currently used for the treatment of cerebral ischemia. The present study aims to investigate the metabolism, pharmacokinetics, and excretion of NBP in humans and identify the enzymes responsible for the formation of major metabolites.
Kate M Ehrensberger et al.
The Journal of biological chemistry, 288(2), 759-769 (2012-12-12)
In yeast, Adh1 (alcohol dehydrogenase 1) is an abundant zinc-binding protein that is required for the conversion of acetaldehyde to ethanol. Through transcriptome profiling of the Schizosaccharomyces pombe genome, we identified a natural antisense transcript at the adh1 locus that
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
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