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Engineering of the critical residues at the stereochemistry-gate loops of Brevibacillus agri dihydropyrimidinase for the production of l-homophenylalanine

Paper ID Volume ID Publish Year Pages File Format Full-Text
35279 45084 2009 7 PDF Available
Title
Engineering of the critical residues at the stereochemistry-gate loops of Brevibacillus agri dihydropyrimidinase for the production of l-homophenylalanine
Abstract

Brevibacillus agri dihydropyrimidinase (BaDHP) exhibits a substrate preference for d-homophenylalanylhydantoin (d-HPAH). Site-directed mutagenesis of BaDHP was performed specifically to the residues proposed to be important in the enzyme activity. M63A, F65A, L94A, L159A and L159V variants exhibited the increased activity (54–469%) toward l-HPAH. L159V variant was used to convert HPAH to l-homophenylalanine (l-HPA) in the hydantoinase process. As compared with the wild-type enzyme, the conversion yield of l-HPA was increased from 39 to 61% by L159V variant. The conversion yield for l-HPA production was further increased up to 90% by coupling L159V variant with Bacillus kaustophilusl-N-carbamoylase and Deinococcus radiodurans N-acylamino acid racemase in the biocatalysis process.

Keywords
l-Homophenylalanine; Dihydropyrimidinase; l-N-Carbamoylase; N-Acylamino acid racemase; Site-directed mutagenesis; Bioconversion
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Engineering of the critical residues at the stereochemistry-gate loops of Brevibacillus agri dihydropyrimidinase for the production of l-homophenylalanine
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 44, Issue 3, March 2009, Pages 309–315
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
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us