55689
Alcohol Dehydrogenase equine
recombinant, expressed in E. coli, ≥0.5 U/mg
Synonym(s):
ADH
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About This Item
Recommended Products
biological source
equine
Quality Level
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.
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.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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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)
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)
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