Restriction enzyme TaqI catalytic rate (Kcat)

Value 2.9 min^-1
Organism Unspecified
Reference Zebala JA, Choi J, Barany F. Characterization of steady state, single-turnover, and binding kinetics of the TaqI restriction endonuclease. J Biol Chem. 1992 Apr 25 267(12):8097-105. p.8100 right column 2nd paragraphPubMed ID1569066
Method The steady-state kinetic parameter were obtained by measuring the velocity of the reaction as a function of substrate concentration at 60°C (Fig. 3A). The substrate ranged from 8 to 0.06 times the Km and the ratio of enzyme to substrate was 1:1OO. The Km and kcat values of the enzyme were obtained by computer fit.
Comments Under these conditions, the velocity was a linear function of enzyme concentration over the range of 1.3 to 25 pM TaqI endonuclease (Fig. 3B). The results at 50°C were qualitatively similar giving a Km of 53 nM and a kcat of 1.3 min^-1
Entered by Ben Marks
ID 101630