Brand  (β version)

PDB ID: 1EE2

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Ligands
Code Name Style Show Link
CHD Cholic acid PoSSuM
NAD Nicotinamide-adenine-dinucleotide PoSSuM
ZN Zinc ion PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 1EE2   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : THE STRUCTURE OF STEROID-ACTIVE ALCOHOL DEHYDROGENASE AT 1.54 A RESOLUTION
Release Data : 2000-10-27
Compound :
mol_id molecule chains
1 ALCOHOL DEHYDROGENASE A,B
ec: 1.1.1.1
Source :
mol_id organism_scientific organism_common
1 Equus caballus  (taxid:9796) Horse
organ: LIVER
Authors : Adolph, H.W.
Keywords : DEHYDROGENASE, ALCOHOL, NICOTINAMIDE COENZYME, STEROID BINDING, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 1.54 Å )
Citation :

Structural basis for substrate specificity differences of horse liver alcohol dehydrogenase isozymes.

Adolph, H.W.,Zwart, P.,Meijers, R.  et al.
(2000)  Biochemistry  39 : 12885 - 12897

PubMed: 11041853
DOI: 10.1021/bi001376s

Substrate Specificity and Stereoselectivity of Horse Liver Alcohol Dehydrogenase. Kinetic Evaluation of Binding and Activation Parameters Controlling the Catalitic Cycles of Unbranched, Acyclic Secondary Alcohols and Ketones as Substrates of the Native and Active-Site-Specific Co(II)-Substituted Enzyme

Adolph, H.W.,Maurer, P.,Scheinder-Bernlohr, H.  et al.
(1991)  Eur.J.Biochem.  201 : 615 - 625

Preparation and Characterization of Isozymes and Isoforms of Horse Liver Alcohol Dehydrogenase

Hubatsch, I.,Maurer, P.,Engel, D.  et al.
(1995)  J.CHROMATOGR.,A  711 : 105 - 112

DOI: 10.1016/0021-9673(95)00227-E

Electrostatic Effects in the Kinetics of Coenzyme Binding to Isozymes of Alcohol Dehydrogenase from Horse Liver

Adolph, H.W.,Kiefer, M.,Cedergren-Zeppezauer, E.
(1997)  Biochemistry  36 : 8743 - 8754

DOI: 10.1021/bi970398k

Reaction

Chain : A, B
UniProt : P00328 (ADH1S_HORSE)
Reaction: EC: Evidence:
Physiological Direction:
a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH 1.1.1.1 -
-
a secondary alcohol + NAD(+) = a ketone + H(+) + NADH 1.1.1.1 -
-