Mutation of cysteine-295 to alanine in secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus affects the enantioselectivity and substrate specificity …

C Heiss, M Laivenieks, JG Zeikus, RS Phillips

文献索引：Heiss, Christian; Laivenieks, Maris; Zeikus; Phillips, Robert S. Bioorganic and Medicinal Chemistry, 2001 , vol. 9, # 7 p. 1659 - 1666

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被引用次数: 42

摘要

The mutation of Cys-295 to alanine in Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase (SADH) was performed to give C295A SADH, on the basis of molecular modeling studies utilizing the X-ray crystal structure coordinates of the highly homologous T. brockii secondary alcohol dehydrogenase (1YKF. PDB). This mutant SADH has activity for 2- propanol comparable to wild-type SADH. However, the C295A mutation was found to ...