MP Biomedicals™ Alcohol Dehydrogenase from Yeast
Facilitates interconversion between alcohols and aldehydes or ketones with reduction of nicotinamide adenine dinucleotide
Manufacturer: MP Biomedicals™ 10016115
Alcohol dehydrogenases are a group of dehydrogenase enzymes that occur in many organisms. It is a metalloenzyme containing four tightly bound zinc atoms per molecule.Each subunit also contains a second zinc atom (conformational zinc), which stabilizes the enzyme's tertiary structure. Per subunit, there are two distinct active site sulfhydryl groups which can be distinguished on the basis of differential reactivity with iodoacetate and butyl isocyanate. A histidine residue is considered to have an essential role.
CAS Number: 9031-72-5
EC Number: 232-870-4
Format: Off-White Flaky Powder
Optimum pH: For the oxidation of ethanol, pH 8.6-9.0 (the enzyme becomes increasingly unstable at higher pH). For the reduction of acetaldehyde a pH nearer to 7.0 is considered optimum. This reaction is kinetically complex with pH being only one factor determining optimum conditions.
Solubility: Dissolves readily at 5 mg/ml in 0.01 M sodium phosphate pH 7.5 to give a clear colorless solution.
Activators: Sulfyhydryl activating reagents, mercaptoethanol, dithiothreitol, cysteine, etc., and heavy metal chelating reagents.
Stabilizers: Dilute solution of the enzyme may be stabilized by serum albumin, gelatin, and/or glutathione or cysteine. At pH values below 6.0 and above 8.5 the enzyme is increasingly unstable. More concentrated solutions of the enzyme in high purity water, near neutrality, are stable several days at 5oC.
In biotransformation, alcohol dehydrogenases are often used for synthesis of enantiomerically pure stereoisomers of chiral alcohols.
|Heavy Metals, -SH reagents|
|8.6 to 9|
|Synthesis of enantiomerically pure Stereoisomers of chiral Alcohols, biotransformation|