kcat

Activity

Catalytic Rate Constant (kcat)

1/s

Spectrophotometric/Colorimetric Assay

25 mM sodium phosphate

25 °C

7.0

None

None

None

The data were collected with a Perkin-Elmer Lambda 25 spectrophotometer (Perkin-Elmer Italia, Monza, Italy). Steady-state kinetic analyses were performed under initial-rate conditions using the Hanes plot linearization method. For Km values of ≤10 μM, the Km values were determined as Ki values, using nitrocefin as the reporter substrate. Each kinetic value is the mean of five different measurements; errors were <5%.