EC 1.1.1.1 Chemical Properties

RTECS 

SZ5999500

storage temp. 

-20°C

solubility 

H2O: soluble1.0mg/mL, clear to slightly hazy, colorless to faintly yellow

form 

solution

color 

slightly beige

Water Solubility 

Soluble in water.

Sensitive 

Hygroscopic

EPA Substance Registry System

Dehydrogenase, alcohol (9031-72-5)

Safety Information

WGK Germany 

3

F 

3-10-21

TSCA 

Yes

HS Code 

35079090

MSDS

• Language:English Provider:SigmaAldrich

EC 1.1.1.1 Usage And Synthesis

Description

Alcohol dehydrogenases (ADH) (EC 1.1.1.1) 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+.

Properties

The alcohol dehydrogenases comprise a group of several isozymes that catalyse the oxidation of primary and secondary alcohols to aldehydes and ketones, respectively, and also can catalyse the reverse reaction.In mammals this is a redox (reduction/oxidation) reaction involving the coenzyme nicotinamide adenine dinucleotide (NAD+).

Applications

In biotransformation, alcohol dehydrogenases are often used for the synthesis of enantiomerically pure stereoisomers of chiral alcohols.Often, high chemo- and enantioselectivity can be achieved. In fuel cells, alcohol dehydrogenases can be used to catalyze the breakdown of fuel for an ethanol fuel cell. 

Uses

Alcohol dehydrogenase catalyzes the reaction: RCH2OH +NAD+ ? RCHO + NADH + H+ It facilitates the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In biotransformation, alcohol dehydrogenases are often used for the synthesis of enantiomerically pure stereoisomers of chiral alcohols.

General Description

This product has been enhanced for energy efficiency and waste prevention when used in fuel cell research.

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.

EC 1.1.1.1(9031-72-5)Related Product Information

• Ethanol
• Acetaldehyde
• Ferric acetylacetonate
• SALCOMINE
• TRIS(2,2,6,6-TETRAMETHYL-3,5-HEPTANEDIONATO)EUROPIUM(III)
• METHYL ISOCYANOACETATE
• TERT-BUTYL ISOCYANIDE
• TRIS(2,2,6,6-TETRAMETHYL-3,5-HEPTANEDIONATO)DYSPROSIUM(III)
• Benzyl isocyanide
• N-BUTYLISOCYANIDE
• Ethyl isocyanoacetate
• COBALT(II) ACETYLACETONATE
• PHENYLSELENOL
• Cupric acetylacetonate
• Tosylmethyl isocyanide
• 1,1,3,3-TETRAMETHYLBUTYL ISOCYANIDE
• 2,4-PENTANEDIONE, SILVER DERIVATIVE
• OXIDO REDUCTASES