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Accession number;02A0304399
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| Title;Effects of the enzyme's conformational flexibility on its enantioselectivity for enzyme-catalyzed reactions. |
| Author;
WATANABE KEIICHI
(Kobe Univ., Grad. Sch.)
YOSHIDA TAKASHI
(Kobe Univ., Grad. Sch.)
UEJI SHIN'ICHI
(Kobe Univ., Grad. Sch.)
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Journal Title;Abstracts. Symposium on Biofunctional Chemistry
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Journal Code:L0836A
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ISSN:
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VOL.16th;NO.;PAGE.86-87(2001)
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| Figure&Table&Reference; |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;For subtilisin-catalyzed reactions in organic solvents containing a small amount of dimethyl sulfoxide(DMSO) as an additive, the relationship between the enantioselectivity and the conformational flexibility of subtilisin estimated from the ESR spectroscopic study provides the first experimental evidence that the enzyme has the optimum flexibility to produce the maximal enantioselectivity toward the given substrates. Interestingly, the non-natural substrates except for the amino acid derivatives required the large flexibility of subtilisin in order to maximize the enantioselectivity. This fact is explained by the assumption that the rigid conformation of subtilisin in organic solvents may prevent its active site from accepting a non-natural substrate with a structure significantly different from that of a natural one. The mechanistic model for the enzyme's enantiorecognition is proposed by the discussion based on the Michaelis-Menten kinetics for each enantiomer of the ester used. (author abst.) |
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