Basic information Description Properties Applications Safety Supplier Related
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EC 1.1.1.1

Basic information Description Properties Applications Safety Supplier Related

EC 1.1.1.1 Basic information

Product Name:
EC 1.1.1.1
Synonyms:
  • ALCOHOL DEHYDROGENASE extrapure for biochemistry
  • ADH, Alcohol:NAD+ oxidoreductase
  • Alcohol dehydrogenase-Agarose from baker's yeast (S.cerevisiae)
  • Alcohol Dehydrogenase from Candida parapsilosis
  • ADH, Alcohol Dehydrogenase from horse liver, Alcohol:NAD+ oxidoreductase, HLADH
  • Alcohol Dedydrogenase,from Yeast
  • Alcohol dehydrogenase
  • ADH, NAD+ oxidoreductase
CAS:
9031-72-5
MF:
n.a.
MW:
0
EINECS:
232-870-4
Product Categories:
  • Oxidoreductases
  • Specialty Enzymes
  • Oxido-Reductase
  • Biochemistry
  • Enzyme
Mol File:
Mol File
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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
PH
7
biological source
Saccharomyces cerevisiae
Water Solubility 
Soluble in water.
Sensitive 
Hygroscopic
Specific Activity
≥300units/mg protein
EPA Substance Registry System
Dehydrogenase, alcohol (9031-72-5)
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Safety Information

WGK Germany 
3
3-10-21
TSCA 
Yes
HS Code 
35079090

MSDS

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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. 

Chemical Properties

Off-white lyophilized powder, soluble in water, pI 5.4, optimum pH 8.6-9.0 (ethanol oxidation) or 7.0 (aldehyde reduction). Stability: high concentration of nearly neutral enzyme in pure water can be stable for several days at 5℃, unstable in acidic (pH lower than 6.0) and alkaline (pH greater than 8.5) solution; adding glutathione, cysteine or serum albumin to dilute solution can increase its stability; lyophilized powder containing sucrose and phosphate, stored at 4℃ for six months, the vitality is reduced by 10%; crystal suspension containing phosphate, stored at 4℃ for six months, the vitality is reduced by 40%. Crystallized suspension containing phosphate, 40% reduction in viability for six months at 4°C. Activators include mercaptoethanol, dimercaptosuccinol, cysteine and heavy metal chelators; inhibitors include heavy metals and sulfhydryl reagents. Enzymatic reaction: alcohol + coenzyme I ═ aldehyde or ketone + reduced coenzyme I.

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 Preparation Products And Raw materials

Raw materials

Preparation Products

EC 1.1.1.1Supplier

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