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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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SrtB _ΔN26 activity requires a cysteine residue at position 209. To determine if SrtB_ΔN26 activity depended on the cysteine residue at position 209, a C209A substitution was made to create SrtB_ΔN26,C209A. This enzyme was inactive against the FRET peptides when compared with SrtB_ΔN26. Addition at 5 mM of the cysteine protease inhibitor, MTSET, to the reaction also eliminates activity (**corresponds to p < 0.01).