Enzymes play vital roles in life processes. Almost all biochemical reactions are mediated by enzymes. The rate constants of
enzyme kinetics are the most important parameters for the reactions catalyzed by enzymes. In 1902, Adrian Brown proposed a
simple single-substrate-single-product model which contains only three rate constants
k
1,
k
−1 and
k
2. So far, biologists can measure the Michaelis constant
K
M
and the catalytic constant
k
cat
, which actually is equal to
k
2, according to Michaelis–Menten equation. Using temperature jump method or transient state kinetics,
k
1,
k
−1 and
k
2 can be determined. However, these methods are complicated. In this article, we design a novel simple method that could determine
the rate constants
k
1 and
k
−1 based on knowing
k
cat
and
K
M
. Our numerical experiments show that the three rate constants can be calculated rather precisely. Hence, we believe that
biochemists could design experiments to measure the rate constants based on our method.
Keywords Michaelis constant - Catalytic constant - Michaelis–Menten equation
This work was partially supported by the National Natural Science Foundation of China (NSFC) under Grant No. 10771206 and
partially by 973 project (2004CB318000) of P. R. China.