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A9770

Sigma-Aldrich

Aldehyde Dehydrogenase, potassium-activated from yeast

lyophilized powder, ≥10 units/mg protein

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Synonym(s):
ALDH, CoA-independent aldehyde dehydrogenase, m-methylbenzaldehyde dehydrogenase, Aldehyde:NAD[P]+ oxidoreductase
CAS Number:
9028-88-0
Enzyme Commission 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.

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

antibody

Product No.
Description
Pricing

related product

Product No.
Description
Pricing

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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  5. What is the molecular weight of Aldehyde Dehydrogenase, potassium-activated from baker's yeast (S. cerevisiae), product A9770?

    Aldehyde dehydrogenase from bakers yeast, product A9770, is a tetramer consisting of subunits of 57 kDa. The molecular weights of its monomer, dimer, trimer, and tetramer are 57 kDa, 114 kDa, 171 kDa, and 228 kDa respectively. The monomers are thought to be assembled into tetramers in a heterologous square arrangement.

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Novel dehydrogenase catalyzes oxidative hydrolysis of carbon-nitrogen double bonds for hydrazone degradation
Itoh H, et al.
The Journal of biological chemistry, 283(9), 5790-5800 (2008)
Christopher G Bazewicz et al.
Immunology, 156(1), 47-55 (2018-11-06)
The role of aldehyde dehydrogenase (ALDH) in carcinogenesis and resistance to cancer therapies is well known. Mounting evidence also suggests a potentially important role for ALDH in the induction and function of regulatory T (Treg) cells. Treg cells are important
Seung-Kyu Park et al.
Biomedical research (Tokyo, Japan), 30(5), 263-269 (2009-11-06)
Ethanol consumption disturbs the balance between the pro- and anti-oxidant systems of the organism, leading to oxidative stress. Electrolyzed-reduced water (ERW) is widely used by people in East Asia for drinking purposes because of its therapeutic properties including scavenging effect
Paper based biofuel cells: Incorporating enzymatic cascades for ethanol and methanol oxidation
Lau C, et al.
International Journal of Hydrogen Energy, 40(42), 14661-14666 (2015)
Balamurugan Jagadeesan et al.
Microbiology (Reading, England), 156(Pt 9), 2782-2795 (2010-05-29)
Listeria adhesion protein (LAP), an alcohol acetaldehyde dehydrogenase (lmo1634), interacts with host-cell receptor Hsp60 to promote bacterial adhesion during the intestinal phase of Listeria monocytogenes infection. The LAP homologue is present in pathogens (L. monocytogenes, L. ivanovii) and non-pathogens (L.
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