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. 2014 Aug 31;14:219. doi: 10.1186/s12866-014-0219-1

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© Donahue et al.; licensee BioMed Central Ltd. 2014

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Kinetic parameters of SrtB _ΔN26 . In order to determine the in vitro kinetic parameters of SrtB_ΔN26 for the SPKTG and PPKTG motifs, we performed a kinetic analysis of the sortase-catalyzed hydrolysis reaction. A. Progress curves of the SrtB_ΔN26-catalyzed hydrolysis reactions at various concentrations of d-SDSPKTGDN-e [8 (blue ●), 10 (green ▪), 20 (red ▲), 40 (teal ▼), 80 (purple ♦), 160 (yellow ), 200 (black ★), and 240 μM (blue +). The steady state rate (V) was determined by fitting the data to a linear function. B. Plot of V against the concentration of the peptide [S]. Nonlinear regression of these data fitted to Equation 1 resulted in a K _m of 74.7 ± 48.2 μM for d-SDSPKTGDN-e. SrtB_ΔN26 is subject to substrate inhibition at peptide concentrations > 30 μM, which is not expected to be physiologically relevant.

Inline graphic — Kinetic parameters of SrtB _ΔN26 . In order to determine the in vitro kinetic parameters of SrtB_ΔN26 for the SPKTG and PPKTG motifs, we performed a kinetic analysis of the sortase-catalyzed hydrolysis reaction. A. Progress curves of the SrtB_ΔN26-catalyzed hydrolysis reactions at various concentrations of d-SDSPKTGDN-e [8 (blue ●), 10 (green ▪), 20 (red ▲), 40 (teal ▼), 80 (purple ♦), 160 (yellow ), 200 (black ★), and 240 μM (blue +). The steady state rate (V) was determined by fitting the data to a linear function. B. Plot of V against the concentration of the peptide [S]. Nonlinear regression of these data fitted to Equation 1 resulted in a K _m of 74.7 ± 48.2 μM for d-SDSPKTGDN-e. SrtB_ΔN26 is subject to substrate inhibition at peptide concentrations > 30 μM, which is not expected to be physiologically relevant.