ChemicalBook--->CAS DataBase List--->9031-72-5

9031-72-5

9031-72-5 Structure

9031-72-5 Structure
IdentificationBack Directory
[Name]

EC 1.1.1.1
[CAS]

9031-72-5
[Synonyms]

ADH
LKADH
HLADH
EC 1.1.1.1
EC: 1.1.1.1
IUB: 1.1.1.1
KETOREDUCTASE CB
KETOREDUCTASE CP
KETOREDUCTASE RS1
KETOREDUCTASE RS2
KETOREDUCTASE CDX010
KETERODUCTASE CDX013
Dehydrogenase,alcohol
Alcohol dehydrogenase
ADH, NAD+ oxidoreductase
Alcohol Dehydrogenase A8
Alcohol Dehydrogenase A1
Alcohol Dehydrogenase A7
ALCOHOL DEHYDROGENASE CB
ALCOHOL DEHYDROGENASE CP
Alcohol Dehydrogenase A6
Alcohol Dehydrogenase A2
Alcohol Dehydrogenase A4
Alcohol Dehydrogenase A9
Alcohol Dehydrogenase A5
Alcohol Dehydrogenase A3
Alcohol Dehydrogenase A27
Alcohol Dehydrogenase A24
Alcohol Dehydrogenase A17
Alcohol Dehydrogenase A26
Alcohol Dehydrogenase A33
Alcohol Dehydrogenase A15
Alcohol Dehydrogenase A18
Alcohol Dehydrogenase A31
Alcohol Dehydrogenase A34
ALCOHOL DEHYDROGENASE RS1
ALCOHOL DEHYDROGENASE RS2
Alcohol Dehydrogenase A22
Alcohol Dehydrogenase A13
Alcohol Dehydrogenase A23
Alcohol Dehydrogenase A29
Alcohol Dehydrogenase A16
Alcohol Dehydrogenase A14
Alcohol Dehydrogenase A32
Alcohol Dehydrogenase A10
Alcohol Dehydrogenase A25
Alcohol Dehydrogenase A28
Alcohol Dehydrogenase A12
Alcohol Dehydrogenase A21
Alcohol Dehydrogenase A11
Alcohol Dehydrogenase A19
Alcohol Dehydrogenase A35
Alcohol Dehydrogenase A20
Alcohol Dehydrogenase 002
ADA, Alcohol dehydrogenase
Alcohol-dehydrogenase 
ALCOHOL: NAD OXIDOREDUCTASE
ALCOHOL:NAD+ OXIDOREDUCTASE
ALCOHOL DEHYDROGENASE, YEAST
ALCOHOL DEHYDROGENASE CDX010
ALCOHOL DEHYDROGENASE CDX013
NADH Dependent Ketoreductase
Alcohol Dehydrogenase equine
alcoholdehydrogenasefromyeast
ALCOHOL DEHYDROGENASE extrapure
Alcohol Dedydrogenase,from Yeast
ADH, Alcohol:NAD+ oxidoreductase
from Yeast [for Blood alcohol-test]
ADH, Alcohol Dehydrogenase from yeast
ALCOHOL DEHYDROGENASE, FROM YEAST(ADH)
AlcoholDehydrogenaseExYeast(Ec1.1.1.1)
alcohol dehydrogenase from equine liver
ALCOHOL DEHYDROGENASE FROM BAKERS YEAST
ALCOHOL DEHYDROGENASE FROM YEAST LYOPH.&
NADH Dependent Ketoreductase Screening Kit
Alcohol dehydrogenase from yeast, lyophil.
ALCOHOL DEHYDROGENASE (LACTOBACILLUS KEFIR)
ALCOHOL DEHYDROGENASE (RHODOCOCCUS ERYTHROPOLIS)
ALCOHOL DEHYDROGENASE extrapure for biochemistry
ALCOHOL DEHYDROGENASE FROM YEAST, 300U/MG PROTEIN
NADH Dependent Ketoreductase Single Screening Kit
NADH Dependent Ketoreductase Custom Screening Kit
ALCOHOL DEHYDROGENASE FROM HORSE LIVER, ~0.3 U/MG
ALCOHOL DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE
ALCOHOL DEHYDROGENASE,YEASTFOR GEL FILTR ATION CHRO
alcohol dehydrogenase from rhodococcus erythropolis
Alcohol Dehydrogenase from Candida parapsilosis
Alcohol-dehydrogenase from Yeast [for Blood alcohol-test]
ALCOHOL DEHYDROGENASE FROM CANDIDA PARA-PSILOSIS, >4 U/ML*
ALCOHOL DEHYDROGENASE FROM HORSE LIVER V IAL 100MG ~3 U/MG
ALCOHOL DEHYDROGENASE FROM HORSE LIVER V IAL 20 MG ~30 U/ML
ALCOHOL DEHYDROGENASE FROM RHODOCOCCUS ERYTHROPOLIS >20U/ML
Alcohol dehydrogenase [from baker's yeast, 300 units/mg protein]
Alcohol dehydrogenase-Agarose from baker's yeast (S.cerevisiae)
ADH, Alcohol Dehydrogenase from horse liver, Alcohol:NAD+ oxidoreductase, HLADH
ALCOHOL DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE BIOCHEMIKA, POWDER, OFF-WHITE, =250 U MG
Alcohol Dehydrogenase from Saccharomyces cerevisiae,ADH, Alcohol Dehydrogenase from yeast, Alcohol:NAD+ oxidoreductase
[EINECS(EC#)]

232-870-4
[Molecular Formula]

n.a.
[MDL Number]

MFCD00081305
Questions And AnswerBack Directory
[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 PropertiesBack Directory
[RTECS ]

SZ5999500
[storage temp. ]

2-8°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 DataBack Directory
[WGK Germany ]

3
[F ]

3-10-21
[TSCA ]

Yes
[HS Code ]

35079090
Raw materials And Preparation ProductsBack Directory
[Raw materials]

Ammonium sulfate
[Preparation Products]

Retinal
Hazard InformationBack Directory
[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]

We are committed to bringing you?Greener?Alternative Products, which adhere to one or more of The 12 Principles of?Greener?Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in fuel cell research. For more information see the article in biofiles.
[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.
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