ChemicalBook > CAS DataBase List > EC 1.1.1.2

EC 1.1.1.2

Product Name
EC 1.1.1.2
CAS No.
9028-12-0
Chemical Name
EC 1.1.1.2
Synonyms
TBADH;EC 1.1.1.2;KETOREDUCTASE T;KETOREDUCTASE LB;frommicrobialsource;KETOREDUCTASE CDX003;AlcoholdehydrogenaseM;Alcohol dehydrogenases;ALCOHOL DEHYDROGENASE T;ALCOHOL DEHYDROGENASE LB
CBNumber
CB7185643
Formula Weight
0
MOL File
Mol file
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EC 1.1.1.2 Property

storage temp. 
-20°C
form 
powder
color 
white
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Safety

Hazard Codes 
Xn
Risk Statements 
42/43
Safety Statements 
22-36/37-45
WGK Germany 
3
10-21
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Hazard and Precautionary Statements (GHS)

Symbol(GHS)
Signal word
Warning
Hazard statements

H319Causes serious eye irritation

Precautionary statements

P305+P351+P338IF IN EYES: Rinse cautiously with water for several minutes. Remove contact lenses, if present and easy to do. Continuerinsing.

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N-Bromosuccinimide Price

Sigma-Aldrich
Product number
49641
Product name
Alcohol Dehydrogenase, recombinant from E. coli
Purity
≥500 U/mL
Packaging
1ml
Price
$224
Updated
2024/03/01
Sigma-Aldrich
Product number
49641
Product name
Alcohol Dehydrogenase, recombinant from E. coli
Purity
≥500 U/mL
Packaging
5ml
Price
$872
Updated
2024/03/01
Usbiological
Product number
167747
Product name
Alcohol Dehydrogenase, Recombinant
Packaging
200ug
Price
$313
Updated
2021/12/16
American Custom Chemicals Corporation
Product number
ENZ0000055
Product name
(R)-OYNITRILASE PA
Purity
95.00%
Packaging
50MG
Price
$682.78
Updated
2021/12/16
American Custom Chemicals Corporation
Product number
ENZ0000055
Product name
(R)-OYNITRILASE PA
Purity
95.00%
Packaging
250MG
Price
$1017.5
Updated
2021/12/16
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EC 1.1.1.2 Chemical Properties,Usage,Production

Uses

Component of NADH recycling systems. Substrate specificity limited to low molecular weight alcohols.

General Description

Alcohol:NAD+ oxidoreductase.
Alcohol dehydrogenase (ADH) from yeast is a metalloenzyme containing four zinc atoms per molecule. NAD+ is its coenzyme.

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 1.1.1.2 Preparation Products And Raw materials

Raw materials

Preparation Products

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EC 1.1.1.2 Suppliers

Service Chemical Inc.
Tel
--
Fax
--
Email
sales@chemos-group.com
Country
Germany
ProdList
6350
Advantage
71
Julich Chiral Solutions
Tel
--
Fax
--
Email
info@julich.com
Country
Germany
ProdList
212
Advantage
64

9028-12-0, EC 1.1.1.2Related Search:


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  • 9028-12-0
  • 9029-12-0
  • Enzymes, Inhibitors, and Substrates
  • Diagnostic and Analytical Enzymes
  • Application Index
  • Biochemicals and Reagents
  • BioChemical
  • Oxidoreductases
  • Specialty Enzymes