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EC 1.1.1.1

Base Information Edit
  • Chemical Name:EC 1.1.1.1
  • CAS No.:9031-72-5
  • Molecular Formula:n.a.
  • Molecular Weight:
  • Hs Code.:35079090
  • Mol file:9031-72-5.mol
EC 1.1.1.1

Synonyms:3-Methyl-2-buten-1-oldehydrogenase;ADH;ADH (enzyme);Acetaldehyde reductase;Alcoholdehydrogenase;Alcohol dehydrogenase (NAD);Aliphatic alcohol dehydrogenase;E.C. 1.1.1.1;Ethanol dehydrogenase;Ethanol oxidoreductase;NAD-dependent alc.dehydrogenase;NAD-dependent alcohol dehydrogenase;NAD-specific aromaticalcohol dehydrogenase;NADH-alcohol dehydrogenase;NADH-aldehyde reductase;Phenylethanol dehydrogenase;Primary alcohol dehydrogenase;

Suppliers and Price of EC 1.1.1.1
Supply Marketing:Edit
Business phase:
The product has achieved commercial mass production*data from LookChem market partment
Manufacturers and distributors:
  • Manufacture/Brand
  • Chemicals and raw materials
  • Packaging
  • price
  • TCI Chemical
  • Alcohol-dehydrogenase from Yeast[for Blood alcohol-test]
  • 10mg
  • $ 79.00
  • Sigma-Aldrich
  • Alcohol Dehydrogenase from Saccharomyces cerevisiae lyophilized powder (contains buffer salts), ≥300?units/mg protein
  • 300000 units
  • $ 548.00
  • Sigma-Aldrich
  • Alcohol Dehydrogenase equine recombinant, expressed in E. coli, ≥0.5 U/mg
  • 500mg
  • $ 543.00
  • Sigma-Aldrich
  • Alcohol Dehydrogenase from Saccharomyces cerevisiae lyophilized powder (contains buffer salts), ≥300units/mg protein
  • 300ku
  • $ 527.00
  • Sigma-Aldrich
  • Alcohol Dehydrogenase from Saccharomyces cerevisiae ≥300?units/mg protein
  • 150000 units
  • $ 693.00
  • Sigma-Aldrich
  • Alcohol Dehydrogenase from Saccharomyces cerevisiae ≥300?units/mg protein
  • 7500 units
  • $ 57.50
  • Sigma-Aldrich
  • Alcohol Dehydrogenase from Saccharomyces cerevisiae ≥300 units/mg protein
  • 7.5ku
  • $ 55.30
  • Sigma-Aldrich
  • Alcohol Dehydrogenase from Saccharomyces cerevisiae lyophilized powder (contains buffer salts), ≥300units/mg protein
  • 7.5ku
  • $ 55.30
  • Sigma-Aldrich
  • Alcohol Dehydrogenase from Saccharomyces cerevisiae lyophilized powder (contains buffer salts), ≥300?units/mg protein
  • 15000 units
  • $ 52.50
  • Sigma-Aldrich
  • Alcohol Dehydrogenase from Saccharomyces cerevisiae ≥300 units/mg protein
  • 15ku
  • $ 50.60
Total 71 raw suppliers
Chemical Property of EC 1.1.1.1 Edit
Chemical Property:
  • Appearance/Colour:solution 
  • PSA:0.00000 
  • LogP:0.00000 
  • Storage Temp.:2-8°C 
  • Sensitive.:Hygroscopic 
  • Solubility.:H2O: soluble1.0mg/mL, clear to slightly hazy, colorless to faint 
  • Water Solubility.:Soluble in water. 
Purity/Quality:

98%,99%, *data from raw suppliers

Alcohol-dehydrogenase from Yeast[for Blood alcohol-test] *data from reagent suppliers

Safty Information:
  • Pictogram(s):  
  • Hazard Codes: 
MSDS Files:

SDS file from LookChem

Total 1 MSDS from other Authors

Useful:
  • 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+.
  • 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.
Technology Process of EC 1.1.1.1

There total 1 articles about EC 1.1.1.1 which guide to synthetic route it. The literature collected by LookChem mainly comes from the sharing of users and the free literature resources found by Internet computing technology. We keep the original model of the professional version of literature to make it easier and faster for users to retrieve and use. At the same time, we analyze and calculate the most feasible synthesis route with the highest yield for your reference as below:

synthetic route:
Guidance literature:
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