Functional and structural responses of liver alcohol dehydrogenase to lysine modifications |
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Authors: | C.S. Tsai D.J. Senior J.H. White J.L. Pitt |
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Affiliation: | 1. Department of Chemistry, Carleton University, Ottawa, Ontario K1S 5B6, Canada;2. Institute of Biochemistry, Carleton University, Ottawa, Ontario K1S 5B6, Canada |
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Abstract: | Acetylation, glycosylation, and methylation, which modify lysine residues of horse liver alcohol dehydrogenase, have been investigated. Acetylation reacted with approximately two-third of the total lysines to induce the greatest structural changes of the enzyme. Glycosylation modified only one lysine residue selectively with indiscernible structural changes. The glycosylation effect was very specific with respect to diastereoisomers for aldopentoses, aldohexoses, and ketohexoses. Methylation produced the largest enhancement in the oxidative activity, which is related to the stability of the modified enzyme to prolonged modification and thermal denaturation. Kinetic studies revealed that a change in the maximal velocity was primarily responsible for the observed activity differences in the modifications. |
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