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Designing the substrate specificity of d-hydantoinase using a rational approach

Paper ID Volume ID Publish Year Pages File Format Full-Text
17678 42688 2009 6 PDF Available
Title
Designing the substrate specificity of d-hydantoinase using a rational approach
Abstract

Enzymes that exhibit superior catalytic activity, stability and substrate specificity are highly desirable for industrial applications. These goals prompted the designed substrate specificity of Bacillus stearothermophilusd-hydantoinase toward the target substrate hydroxyphenylhydantoin (HPH). Positions crucial to substrate specificity were selected using structural and mechanistic information on the structural loops at the active site. The size and hydrophobicity of the involved amino acids were rationally changed, and the substrate specificities of the designed d-Hyd mutants were investigated. As a result, M63I/F159S exhibited about 200-fold higher specificity for HPH than the wild-type enzyme. Systematic mutational analysis and computational modeling also supported the rationale used in the design.

Keywords
Rational design; d-Hydantoinase; Non-natural d-amino acid; Substrate specificity; Hydroxyphenylhydantoin
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 44, Issue 3, 5 March 2009, Pages 170–175
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
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