| Autor: |
de Kok PM; Department of Organic Chemistry, Eindhoven University of Technology, The Netherlands., Beijer NA, Buck HM, Sluyterman LA, Meijer EM |
| Jazyk: |
angličtina |
| Zdroj: |
European journal of biochemistry [Eur J Biochem] 1988 Aug 15; Vol. 175 (3), pp. 581-5. |
| DOI: |
10.1111/j.1432-1033.1988.tb14231.x |
| Abstrakt: |
The geometry of seven NAD+ analogues bound to horse liver alcohol dehydrogenase (LADH) modified only in their nicotinamide group, have been studied using AMBER molecular mechanics energy-minimization procedures. Starting geometries were taken from X-ray crystallographic data for NAD+/Me2SO/LADH reported by Eklund and co-workers. In this study the NAD+ analogues were encaged by the constituent amino acids of the enzyme within a range of 0.6 nm from the initial NAD+/Me2SO/Zn2+ complex. The calculational method used is able to rationalize individual substituent effects and to evaluate the essential interactions between NAD+ analogue, enzyme, Me2SO and Zn2+ without the necessity of additional X-ray data. The results presented here demonstrate that the reactivity of NAD+ derivatives as reported in literature can be qualitatively related to the position of the pyridine moiety in the active site. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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