Abstract
A spectrophotometric method to measure hydrolysis of the bacterial second messenger cyclic dimeric guanosine monophosphate is described for characterization of enzymes under aerobic and anaerobic conditions. The method allows for obtaining all necessary data to calculate KM and kcat from reactions within a single 96-well plate that can be measured using a standard plate reader. The spectrophotometric assay has been used to measure the rates and obtain Michaelis-Menten parameters for the c-di-GMP phosphodiesterase DcpG with the sensor domain in various ligation states.
Full Text
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call