Cover Feature: Combined MD and QM/MM Calculations Reveal Allostery‐Driven Promiscuity in Dipeptide Epimerases of Enolase Family (Chem. Asian J. 16/2022)

A single site mutation can induce functional promiscuity in homoserine kinase

“…7,8 Mechanistic studies of enzyme promiscuity show that some strategic mutations change the substrate recognition pattern, which, in turn, causes promiscuity in enzymes. [9][10][11] However, some special cases do also exist where a single site mutation causes functional diversity where an enzyme catalyzes an entirely new function without compromising its binding site topology. [12][13][14] Homoserine kinase (HSK) is an enzyme with such peculiarity.…”