Alternative binding modes in abortive NADH-alcohol complexes of horse liver alcohol dehydrogenase.

ABSTRACT: Enzymes typically have high specificity for their substrates, but the structures of substrates and products differ, and multiple modes of binding are observed. In this study, high resolution X-ray crystallography of complexes with NADH and alcohols show alternative modes of binding in the active site. Enzyme crystallized with the good substrates NAD⁺ and 4-methylbenzyl alcohol was found to be an abortive complex of NADH with 4-methylbenzyl alcohol rotated to a "non-productive" mode as compared to the structures that resemble reactive Michaelis complexes with NAD⁺ and 2,2,2-trifluoroethanol or 2,3,4,5,6-pentafluorobenzyl alcohol. The NADH is formed by reduction of the NAD⁺ with the alcohol during the crystallization. The same structure was also formed by dir

SUBMITTER: Plapp BV 

PROVIDER: S-EPMC7980771 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature