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Updated: Feb 15, 2026

Millifluidics for Chemical Synthesis and Time-resolved Mechanistic Studies
Published on: November 27, 2013
PLP-independent racemization: mechanistic and mutational studies of O-ureidoserine racemase (DcsC)
Yeong-Chan Ahn1, Conrad Fischer, Marco J van Belkum
1Department of Chemistry, University of Alberta, Edmonton, AB, CanadaT6G 2G2. john.vederas@ualberta.ca.
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.
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