Skip to Content
Merck
All Photos(1)

Documents

55689

Sigma-Aldrich

Alcohol Dehydrogenase equine

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

Synonym(s):

ADH

Sign Into View Organizational & Contract Pricing
All Photos(1)

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)

Looking for similar products? Visit Product Comparison Guide

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)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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
Horse Liver Alcohol Dehydrogenase-Catalyzed Aldehyde Oxidation
Oppenheimer NJ and Henehan G TM
The Journal of Biological Chemistry, 407-415 (1995)
Ethanol metabolism and implications for disease
Rajendram R, et al.
Neuropathology of Drug Addictions and Substance Misuse, 377-388 (2016)
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)
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)
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service