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55689

Sigma-Aldrich

Alcohol Dehydrogenase equine

recombinant, expressed in E. coli, ≥0.5 U/mg

Synonym(s):

ADH

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About This Item

CAS Number:
9031-72-5
Enzyme Commission number:
1.1.1.1 (BRENDA, IUBMB)
EC Number:
232-870-4
MDL number:
MFCD00081305
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

equine

Quality Level

100

recombinant

expressed in E. coli

description

Isozyme E sequence

form

lyophilized powder

specific activity

≥0.5 U/mg

color

white
light yellow

pH

7

solubility

water: 5 mg/mL

application(s)

life science and biopharma

storage temp.

−20°C

Gene Information

equine ... ADH1(111772995)

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General description

Research Area: Neuroscience
Alcohol dehydrogenase is a zinc metalloprotein that forms five classes of isoenzymes through the dimerization of eight different subunits.

Application

Alcohol Dehydrogenase equine has been used in in vitro alcohol dehydrogenase (Adh) assay.

Biochem/physiol Actions

Alcohol dehydrogenase catalyzes the oxidative conversion of alcohol into aldehyde. It has a homodimeric structure with a co-enzyme binding domain at the C-terminal and an N-terminal catalytic domain. The active site is located at the interdomain cleft. Binding of NAD+ in the active site causes conformational changes which create the binding site for the alcohol substrate.
Horse liver alcohol dehydrogenase (HL-ADH) is an enzyme with broad specificity, capable of catalyzing the reversible oxidation of a wide variety of primary and secondary alcohols to form their corresponding aldehydes and ketones. Moreover, alcohol dehydrogenase can oxidize ethanol while simultaneously reducing nicotinamide adenine dinucleotide (NAD+) to NADH. Previous studies have demonstrated that ADH and ALDH variants can influence alcohol dependence. Additionally, the ADH genotype has been linked to lacunar infarction and neuropsychiatric diseases.

Unit Definition

1 U corresponds to the amount of enzyme which reduces 1 μmol benzaldehyde per minute at pH 7.0 and 30 °C.

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

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Ethanol metabolism and implications for disease
Rajendram R, et al.
Neuropathology of Drug Addictions and Substance Misuse, 377-388 (2016)
Horse Liver Alcohol Dehydrogenase-Catalyzed Aldehyde Oxidation
Oppenheimer NJ and Henehan G TM
The Journal of Biological Chemistry, 407-415 (1995)
Ioanna A Gorbunova et al.
The journal of physical chemistry. B, 125(34), 9692-9707 (2021-08-20)
The dynamics of polarized fluorescence in NADH in alcohol dehydrogenase (ADH) in buffer solution has been studied using the TCSPC spectroscopy. A global fit procedure was used for determination of the fluorescence parameters from experiment. The interpretation of the results
In vitro activation of NAD-dependent alcohol dehydrogenases by Nudix hydrolases is more widespread than assumed
Ochsner AM, et al.
Febs Letters, 588(17), 2993-2999 (2014)
Association study of alcohol dehydrogenase and aldehyde dehydrogenase polymorphism with Alzheimer disease in the Taiwanese population
Wu YY, et al.
Frontiers in Neuroscience, 15, 625885-625885 (2021)
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