MP Biomedicals™ Alcohol Dehydrogenase from Yeast

Description

• 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.