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Recombinant Alcohol dehydrogenase from E. coli

 Product Information

Cat #
MBS-1038
CAS No.
9031-72-5
Enzyme Commission Number
EC 1.1.1.1
Product Overview
High-quality enzyme products. Well-defined strains can be also provided for our clients to manufacture fermented products in a cost-effective way.
Features
Ready-to-use product, accelerating research progress, enhancing application performance.
Method
Technology
Synonyms
aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase
Type
Function
A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
Applications
Research and Development
Storage
Store at 4°C. Do not store the enzyme in presence of sodium azide.
Storage Buffer
Shelf Life
Strains
Escherichia coli
Source
E. coli
Appearance
Molecular Weight
~ 38,642 Da
Color / Form
Instruction
Enzyme Class
Oxidoreductases
Production Methods
Fermentation
Activity
6.7 U/mg protein at pH 8.5 and 25°C.
Specific Enzyme Activity
Purity
Unit Definition
One Unit of alcohol dehydrogenase is defined as the amount of enzyme required to produce one µmole of NADH from NAD+.
Amino Acids Sequence
WARNINGS
Shipping
Formula
Reaction
(1) a primary alcohol + NAD+ = an aldehyde + NADH + H+
(2) a secondary alcohol + NAD+ = a ketone + NADH + H+
Recommendation
Species Reactivity
Contents
Compatibility
Melting Point
Final Titre
Fermentation Time
Recovery Yield
Starting Material
Specification
On customer requests
Substrates
Concentration
Usage And Dosage
Product Type
Enzymes

 Description

Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+.

For Research Use Only.
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