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

文献情報

出版日 2018-01-24

DOI 10.1039/C7OB03013D

インパクトファクター 3.876

著者

Yeong-Chan Ahn, Conrad Fischer, Marco J. van Belkum, John C. Vederas

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要旨

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.

掲載誌

Organic & Biomolecular Chemistry

CiteScore: 3.4

自己引用率: 10.3%

年間論文数: 1041

Organic & Biomolecular Chemistry (OBC) publishes original and high impact research and reviews in organic chemistry. We welcome research that shows new or significantly improved protocols or methodologies in total synthesis, synthetic methodology or physical and theoretical organic chemistry as well as research that shows a significant advance in the organic chemistry or molecular design aspects of chemical biology, catalysis, supramolecular and macromolecular chemistry, theoretical chemistry, mechanism-oriented physical organic chemistry, medicinal chemistry or natural products. Articles published in the journal should report new work which makes a highly-significant impact in the field. Routine and incremental work is generally not suitable for publication in the journal. More details about key areas of our scope are below. In all cases authors should include in their article clear rationale for why their research has been carried out.

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

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