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Issue 7, 2018
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PLP-independent racemization: mechanistic and mutational studies of O-ureidoserine racemase (DcsC)

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Abstract

O-Ureidoserine racemase (DcsC) is a PLP-independent enzyme in the biosynthetic route to the antibiotic D-cycloserine. Here we present the recombinant expression and characterization of a significantly more active DcsC variant featuring an N-terminal SUMO-tag. Synthesis of enantiomeric pure inhibitors in combination with site-specific mutation of active site cysteines to serines of this enzyme offers closer insights into the mechanism of this transformation. Homology modelling with a close relative (diaminopimelate epimerase, DapF) inspired C- and N-terminal truncation of DcsC to produce a more compact yet still active enzyme variant.

Graphical abstract: PLP-independent racemization: mechanistic and mutational studies of O-ureidoserine racemase (DcsC)

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Supplementary files

Article information


Submitted
05 Dec 2017
Accepted
16 Jan 2018
First published
24 Jan 2018

Org. Biomol. Chem., 2018,16, 1126-1133
Article type
Paper

PLP-independent racemization: mechanistic and mutational studies of O-ureidoserine racemase (DcsC)

Y. Ahn, C. Fischer, M. J. van Belkum and J. C. Vederas, Org. Biomol. Chem., 2018, 16, 1126
DOI: 10.1039/C7OB03013D

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