Aldehyde Dehydrogenase, potassium-activated from yeast (C15-1291-504)

General description

Aldehyde dehydrogenase, from yeast, is used to catalyze the oxidation of a wide range of substrates, such as acetaldehyde, formaldehyde, propionaldehyde, n-butylaldehyde, isobutylaldehyde, n-valeraldehyde, caproaldehyde, benzaldehyde, glycoaldehyde, D-glyceraldehyde, malonic semialdehyde, and succinic aldehyde. Aldehyde dehydrogenase, from yeast has been used to study the production of ethanol and isobutanol. Aldehyde dehydrogenase, from Sigma, has been used along with alcohol dehydrogenase to measure ethanol production during the characterization of glycolytic metabolism and ion transport in Candida albicans.

The family of aldehyde dehydrogenase (ALDH) contains 19 genes in humans. It is localized in the nucleus, cytosol, mitochondria and endoplasmic reticulum of the cell.

Research area: Cell Signaling

Application

Aldehyde Dehydrogenase, potassium-activated from yeast has been used:

• for enzyme immobilization and to oxidize formaldehyde to formate
• to study the functional relation between hydrazone
• to measure ethanol production.

Biochem/physiol Actions

Aldehyde dehydrogenase (ALDH) modulates the non-P450 aldehyde reduction enzyme system. It protects the cell from the effects of toxic aldehydes. Mutations in this gene leads to Sjogren‐Larsson syndrome, Larsson syndrome, type II hyperprolinemia and cancer. ALDH-2 lowers cardiac ischemia, which arises due to myocardial infarction or post cardiac surgery.Aldehyde Dehydrogenase (ALDH) participates in the functioning of regulatory T cells that are a part of the immune system. It is also involved in cellular detoxification, the amino acid metabolism and protects cells against ultraviolet (UV) rays-induced damage. ALDH plays a role in retinoic acid biosynthesis and signaling.

Aldehyde dehydrogenase is a tetramer and has several different isoforms. 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 tested in 0.01 M pyrophosphate buffer shows a sharp optimum around pH 9.3 with acetaldehyde as substrate.

Unit Definition

One unit will oxidize 1 micromole of acetaldehyde to acetic acid per minute pH 8.0 at 25 deg C.

Physical form

Contains potassium phosphate salts