Conformational changes and catalysis by alcohol dehydrogenase

As shown by X-ray crystallography, horse liver alcohol dehydrogenase undergoes a global conformational change upon binding of NAD + or NADH, involving a rotation of the catalytic domain relative to the coenzyme binding domain and the closing up of the active site to produce a catalytically efficient...

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Veröffentlicht in:	Archives of biochemistry and biophysics 2010-01, Vol.493 (1), p.3-12
1. Verfasser:	Plapp, Bryce V.
Format:	Artikel
Sprache:	eng
Schlagworte:	Alcohol Dehydrogenase - chemistry Alcohol Dehydrogenase - metabolism Amino Acids - chemistry Biocatalysis Crystallography Crystallography, X-Ray Enzyme activation Enzyme mechanism Hydrogen-Ion Concentration Isomerism Kinetic simulation Kinetics Models, Molecular NAD - metabolism Protein Binding Protein Conformation Protein structure Proton relay Zinc coordination
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