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.
Yeast alcohol dehydrogenase (yADH) serves as an excellent model system for enzyme-catalyzed H transfer because unlike many other enzymes, the chemical step, oxidation of a primary alcohol to an aldehyde by NAD+, is rate-limiting with aromatic substrates.
Grade: 2× Crystalline
Specific Activity: ≥300 u/mg protein
Key Applications: Catalysis breakdown of ethanol, Synthesis of enantiomerically pure stereoisomers of chiral alcohols
Application Areas: Enzmology
Product Type: Proteins, Enzymes & Peptides
Extinction Coefficient (E1%): E1%260= 12.6(lit.)
Presentation: Off-White Flaky Powder
Format: Powder
Isoelectric point (pI): 5.4(lit.)
pH: Optimal pH: 8.6-9.0 (lit.)
NOTES: Activators: Sulfyhydryl activating reagents, mercaptoethanol, dithiothreitol, cysteine, etc., and heavy metal chelating reagents. Inhibitors: Heavy metals and -SH 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 5°C.
Specificity: Yeast ADH which has a more narrow specificity than that of liver enzyme, accepts ethanol, is somewhat active on the straight chain primary alcohols, and acts to a very limited extent on certain secondary and branched chain alcohols. NADP does not serve as coenzyme.
Solubility: Dissolves readily at 5 mg/mL in 0.01 M sodium phosphate pH 7.5 to give a clear colorless solution.
Storage & Handling: +4°C