| 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 |