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. 2014 Sep;196(17):3122–3133. doi: 10.1128/JB.01698-14

FIG 2.

FIG 2

Kinetics of WbwCECO104 and WbwCECO5 reactions. The standard assay as described in Materials and Methods was used to measure Gal transfer by purified WbwC enzymes. (A) WbwCECO104 reaction with acceptor 8 (0.25 mM) as a function of UDP-Gal concentration. The apparent Km for UDP-Gal was 0.73 mM with an apparent Vmax of 0.87 μmol/h/mg protein. (B) WbwCECO104 reaction as a function of acceptor 8 concentration. UDP-Gal concentration was 2.2 mM. The apparent Km for 8 was 0.12 mM with an apparent Vmax of 1.57 μmol/h/mg protein. (C) WbwCECO5 reaction with 0.25 mM acceptor 8 as a function of UDP-Gal concentration. The apparent Km for UDP-Gal was 1.20 mM with an apparent Vmax of 2.67 μmol/h/mg protein. (D) WbwCECO5 reaction as a function of acceptor 8. UDP-Gal donor concentration was 1.09 mM. The apparent Km for acceptor 8 was 0.10 mM with an apparent Vmax of 1.42 μmol/h/mg protein. Substrate inhibition was apparent at high acceptor concentration (not shown). All results were analyzed by regression analysis with GraphPad Prism.