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. Author manuscript; available in PMC: 2019 Oct 3.
Published in final edited form as: Mol Microbiol. 2018 Oct 3;110(2):239–261. doi: 10.1111/mmi.14100

Table 1. Comparison of RsBluE and SePduX activities as a function of substrates.

Specific activity values for purified and sarkosyl solubilized RsBluE and SePduX enzymes were assayed for ATPase activity in the presence and absence of L-Thr or L-Ser. Values are reported as mean ± standard deviation of three measurements of activity at 100 mM ATP and 50 mM L-Thr or L-Ser. Activity was measured with a NADH consumption assay (see Materials and Methods).

Protein ATP
(μmol ATP min−1 mg−1)
L-Thr
(μmol ATP min−1 mg−1)
L-Ser
(μmol ATP min−1 mg−1)
RsBluE 0.93 ± 0.02 0.77 ± 0.02 0.42 ± 0.01
SePduX 1.00 ± 0.03 0.91 ± 0.03 0.65 ± 0.02