Cornish-Bowden A
J Theor Biol. 1984 Jun 7;108(3):451-7. doi: 10.1016/s0022-5193(84)80045-4.
If an enzyme catalyses two competing reactions, their relative rates are determined by the concentrations of the competing substrates and the two specificity constants, i.e. the catalytic constants for the two substrates divided by the corresponding Michaelis constants. The concept of a specificity constant can be extended to reactions that require two or more substrates: in such cases the specificity for any competing substrate is determined by the apparent specificity constant measured at whatever concentrations of co-substrates, inhibitors, etc., exist under the conditions of competition. The partitioning between two competing substrates is independent of the concentration of any species, such as co-substrate, inhibitor, etc., that reacts only in the part of the mechanism that is common between the competing substrates.
如果一种酶催化两个相互竞争的反应,它们的相对速率由竞争底物的浓度和两个特异性常数决定,即两种底物的催化常数除以相应的米氏常数。特异性常数的概念可以扩展到需要两种或更多种底物的反应:在这种情况下,对任何竞争底物的特异性由在竞争条件下存在的任何共底物、抑制剂等浓度下测得的表观特异性常数决定。两种竞争底物之间的分配与仅在竞争底物之间共同的机制部分发生反应的任何物种(如共底物、抑制剂等)的浓度无关。