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A9770

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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:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

biological source

yeast

Quality Level

form

lyophilized powder

specific activity

≥10 units/mg protein

storage condition

(Tightly closed. Dry)

color

white

UniProt accession no.

foreign activity

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

storage temp.

2-8°C

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This Item
A6338A7011A3263
specific activity

≥10 units/mg protein

specific activity

≥2.0 units/mg protein

specific activity

≥300 units/mg protein

specific activity

≥300 units/mg protein

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder (contains buffer salts)

form

powder

UniProt accession no.

A0A3G3NDH9, S5RK20, S5RCH3, S5S176

UniProt accession no.

-

UniProt accession no.

A0A3G3NDH9, S5RCH3, S5RK20, S5S176

UniProt accession no.

A0A3G3NDH9, S5RCH3, S5RK20, S5S176

storage condition

(Tightly closed. Dry)

storage condition

-

storage condition

(Keep container tightly closed in a dry and well-ventilated place.)

storage condition

(Tightly closed. Dry)

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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
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)
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)
Xabier Marichalar-Mendia et al.
Oral oncology, 46(1), 9-13 (2009-11-10)
Oral cancer is the sixth most common cancer worldwide and a major health problem in some parts of the world. Epidemiological studies have shown that habitual alcohol consumption could be a risk factor in oral carcinogenesis, although the true involvement
P I Nikel et al.
Journal of applied microbiology, 109(2), 492-504 (2010-02-13)
Analysis of the physiology and metabolism of Escherichia coli arcA and creC mutants expressing a bifunctional alcohol-acetaldehyde dehydrogenase from Leuconostoc mesenteroides growing on glycerol under oxygen-restricted conditions. The effect of an ldhA mutation and different growth medium modifications was also

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