view article
Figure 1
Biochemical comparison of AlrV and BsrV from V. cholerae. (a) Predicted protein features of the monospecific alanine racemase (AlrV) and broad-spectrum racemase (BsrV) from V. cholerae generated with the NCBI protein-analysis package. Dimerization motifs are in yellow. SP, signal peptide. Red circles pinpoint the catalytic Lys and Tyr residues. Vertical lines correspond to conserved functional residues (PLP binding, substrate binding, catalytic site and dimeric interface). (b) Schematic of the different methods used to assess amino-acid racemase activities (see §[link]2). (c, d) D-Amino-acid accumulation in the presence of AlrV (c) and BsrV (d) after 90 min reactions with various substrates revealed through Marfey's derivatization. The results in (c) and (d) are the means ± SD of triplicates from two independent experiments. See also Supplementary Fig. S1.

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
Volume 70| Part 1| December 2014| Pages 79-90
doi:10.1107/S1399004713024838
Follow Acta Cryst. D
Sign up for e-alerts
E-alerts
Follow Acta Cryst. on Twitter
Twitter
Follow us on facebook
Facebook
Sign up for RSS feeds
RSS