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KMID : 1094720160210030364
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Biotechnology and Bioprocess Engineering
2016 Volume.21 No. 3 p.364 ~ p.372
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Structural basis for the substrate specificity of 3-hydroxybutyrate dehydrogenase
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Yeon Young-Joo
Park Hyung-Yeon
Park Kyung-Moon
Park Hyun-June
Yoo Young-Je
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Abstract
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The substrate specificity of 3-hydroxybutyrate dehydrogenase from Alcaligenes faecalis with a non-native substrate, levulinic acid, was studied by analysis of the enzyme-substrate molecular interactions. The relation between structural and kinetic parameters was investigated considering the catalytic mechanism of the enzyme. The effects of key positive mutations (H144L, H144L/W187F) on the catalytic activity of the enzyme were studied by employing a surface analysis of its interatomic contacts between the enzyme and substrate atoms. The results revealed that the alteration of hydrogen bond network and rearrangement of the hydrophobic interactions between the active site and substrate molecule are the key structural basis for the change of the substrate specificity of 3-hydroxybutyrate dehydrogenase toward levulinic acid. With this approach, the structural basis for the substrate specificity of the enzyme could be elucidated in a quantitative manner.
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KEYWORD
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3-hydroxybutyrate dehydrogenase, interatomic contact surface, levulinic acid, molecular docking, substrate specificity
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