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A9770

Sigma-Aldrich

Aldehyde Dehydrogenase, potassium-activated from yeast

lyophilized powder, ≥10 units/mg protein

Synonym(s):

ALDH, CoA-independent aldehyde dehydrogenase, m-methylbenzaldehyde dehydrogenase, Aldehyde:NAD[P]+ oxidoreductase

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About This Item

CAS Number:
9028-88-0
EC Number:
1.2.1.5 (BRENDA, IUBMB)
EC Number:
232-846-3
MDL number:
MFCD00081306
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

yeast

Quality Level

200

form

lyophilized powder

specific activity

≥10 units/mg protein

storage condition

(Tightly closed. Dry)

color

white

UniProt accession no.

A0A3G3NDH9
S5RCH3
S5RK20
S5S176

foreign activity

NADH oxidase ≤0.01%
NADPH oxidase ≤0.01%
alcohol dehydrogenase ≤0.01%
lactic dehydrogenase ≤0.01%

storage temp.

2-8°C

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.[1]

Research area: Cell Signaling

Application

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

  • for enzyme immobilization and to oxidize formaldehyde to formate[2]
  • to study the functional relation between hydrazone[3]
  • to measure ethanol production[4].

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.[1] ALDH-2 lowers cardiac ischemia, which arises due to myocardial infarction or post cardiac surgery.[5]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.[6]
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.[7]

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Certificates of Analysis (COA)

Lot/Batch Number
0000396780
0000396001
0000396002
0000396003
0000388003

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