Structural basis for the substrate specificity of 3-hydroxybutyrate dehydrogenase |
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| Authors: | Young Joo Yeon Hyung-Yeon Park Kyungmoon Park Hyun June Park Young Je Yoo |
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| Affiliation: | 1.The Institute of Molecular Biology and Genetics,Seoul National University,Seoul,Korea;2.School of Chemical and Biological Engineering,Seoul National University,Seoul,Korea;3.Bio-MAX Institute,Seoul National University,Seoul,Korea;4.Department of Biological and Chemical Engineering,Hongik University,Sejong,Korea |
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| Abstract: | 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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