Aldehyde dehydrogenase belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor.
Aldehyde dehydrogenase oxidizes a number of aliphatic and aromatic aldehydes. Acetyl-GSH is not hydrolyzed.
Aldehyde dehydrogenase is a tetramer and has several different isoforms. The enzyme tested in 0.01 M pyrophosphate buffer shows a sharp optimum around pH 9.3 with acetaldehyde as substrate. Potassium ions and cysteine are essential for the enzyme′s activity. Rubidium or NH4+ can be substituted for K+, and glutathione for cysteine. Lithium, Na+, and Cs+ inhibit the reaction. Aldehyde dehydrogenase is inhibited by propylurea, crotonaldehyde, n-propyl isocyanate, cyclohexyl isocyanate, 1-n-propyl-1-[(4-chlorophenyl)sulphonyl]-3-n-propylurea, and 1-methyl-1-[(4-chlorophenyl)sulphonyl]-3-n-propylurea. The enzyme may be utilized to quantitate aldehydes present in blood.
Specific Activity: Protein-~5 u/mg, solid-≥1 u/mg solid
Key Applications: Acting on aldehydes or oxo groups
Product Type: Proteins, Enzymes & Peptides
Gene Id: 855205
Uniport Number: P54114
Biochemical Category: Proteins, Enzymes & Peptides
Extinction Coefficient (E1%): 9.4 (279 nm)(Lit)
Presentation: Off white powder
Format: Potassium Activated, Freeze dried stabilized powder
pH: Optimum pH: 9.0
Solubility: Dissolves readily at 5 mg/mL in 0.1M Tris/HCI pH 8.0 to give a clear colorless solution.
Storage & Handling: Store at -20°C, Desiccated.