Molecular transform quantization of enzyme surface probes
James W. King, Ronald J. Kassel · International Journal of Quantum Chemistry · 1992
Inhibition of enzyme function by series of appropriate substrates is the first step in the classical approach to definition of the reactive or binding sites on an enzyme surface. Several years ago, M. I. Kabachnik and his colleagues published inhibition rate data for acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) by phosphonates and phosphates. Some of the phosphonate data has been reexamined from a structure-activity point of view using the square root of the integrated molecular transform as a unitary structure descriptor. Linear regressions showed good correlation in the BuChE case; less adequate correlation were manifested with the AChE data. This is attributable to the predominantly lipophilic nature of the interaction between BuChE and substrates as compared to AChE, where electronic factors may have a prominent role. The correlation further suggest a different, but nontrivial, mode of action between the respective enzymes and their substrates. © 1992 John Wiley & Sons, Inc.