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55689

Sigma-Aldrich

Alcohol Dehydrogenase equine

recombinant, expressed in E. coli, ≥0.5 U/mg

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Synonym(s):
ADH
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:

recombinant

expressed in E. coli

Quality Level

description

Isozyme E sequence

form

lyophilized powder

specific activity

≥0.5 U/mg

storage temp.

−20°C

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This Item
A8656A701174931
Sigma-Aldrich

55689

Alcohol Dehydrogenase equine

Sigma-Aldrich

74931

Alcohol Dehydrogenase

form

lyophilized powder

form

powder

form

lyophilized powder (contains buffer salts)

form

powder

recombinant

expressed in E. coli

recombinant

-

recombinant

-

recombinant

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

Quality Level

100

Quality Level

200

Quality Level

300

Quality Level

-

description

Isozyme E sequence

description

-

description

-

description

-

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.

Unit Definition

1 U corresponds to the amount of enzyme which reduces 1 μmol benzaldehyde per minute at pH 7.0 and 30 °C.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Ioanna A Gorbunova et al.
The journal of physical chemistry. B, 125(34), 9692-9707 (2021-08-20)
The dynamics of polarized fluorescence in NADH in alcohol dehydrogenase (ADH) in buffer solution has been studied using the TCSPC spectroscopy. A global fit procedure was used for determination of the fluorescence parameters from experiment. The interpretation of the results
Liliya S Chernova et al.
RSC advances, 10(14), 8364-8376 (2020-02-26)
Small heat shock proteins (sHSPs) are ubiquitous molecular chaperones preventing the irreversible denaturation of proteins. While in Escherichia coli two sHSPs IbpA and IbpB work in strong cooperation, the sole Mollicute with free-living ability Acholeplasma laidlawii carries a single gene
F Colonna-Cesari et al.
The Journal of biological chemistry, 261(32), 15273-15280 (1986-11-15)
A study of the hinge bending mode in the enzyme liver alcohol dehydrogenase is made by use of empirical energy functions. The enzyme is a dimer, with each monomer composed of a coenzyme binding domain and a catalytic domain with
H Eklund et al.
Biochemistry, 23(25), 5982-5996 (1984-12-04)
The binding of NAD to liver alcohol dehydrogenase has been studied in four different ternary complexes by using crystallographic methods. These complexes crystallize isomorphously in a triclinic crystal form which contains the whole dimer of the enzyme in the asymmetric
Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 A resolution.
H Eklund et al.
Journal of molecular biology, 146(4), 561-587 (1981-03-15)

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