A9770
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
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biological source
yeast
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
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
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
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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
Certificates of Analysis (COA)
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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)
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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
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Xiao-Jun Ji et al.
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Ethanol was a major byproduct of 2,3-butanediol (2,3-BD) fermentation by Klebsiella oxytoca ME-UD-3. In order to achieve a high efficiency of 2,3-BD production, K. oxytoca mutants deficient in ethanol formation were successfully constructed by replace the aldA gene coding for
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