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A single Phe54Tyr substitution improves the catalytic activity and thermostability of Trigonopsis variabilisd-amino acid oxidase

Paper ID Volume ID Publish Year Pages File Format Full-Text
33581 44985 2010 7 PDF Available
Title
A single Phe54Tyr substitution improves the catalytic activity and thermostability of Trigonopsis variabilisd-amino acid oxidase
Abstract

The industrial importance of Trigonopsis variabilisd-amino acid oxidase (TvDAAO) is represented by its biocatalytic oxidative deamination of cephalosporin C (CPC) to yield glutaryl-7-aminocephalosporanic acid (GL-7-ACA). The process has been incorporated into a two-step bioconversion to produce 7-aminocephalosporanic acid, the crucial synthetic nucleus for several semi-synthetic cephalosporin antibiotics. A homology model of TvDAAO indicated that residue F54 is in a close proximity to the in silico docked CPC. Substitution of this F54 to Tyr (F54Y) resulted in 6-fold improvement in kcat,app and ∼2.5-fold increase in Ki of GL-7-ACA. Heat treatment (55°C, 60 min) did not decrease the activity of F54Y. It is suggested that the Tyr substitution might initiate hydrogen bond formation with the amino group of CPC and facilitate deamination. Faster substrate turnover, reduced GL-7-ACA inhibition and improved thermostability of the F54Y substitution render it a useful candidate in industrial production of semi-synthetic cephems.

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A single Phe54Tyr substitution improves the catalytic activity and thermostability of Trigonopsis variabilisd-amino acid oxidase
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Publisher
Database: Elsevier - ScienceDirect
Journal: New Biotechnology - Volume 27, Issue 1, 28 February 2010, Pages 78–84
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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You save - $31
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