Bal W, Bertini I, Kozlowski H, Monnanni R, Scozzafava A, Siatecki G Z
Institute of Chemistry, University of Wroclaw, Poland.
J Inorg Biochem. 1990 Nov;40(3):227-35. doi: 10.1016/0162-0134(90)80056-4.
The molecular (1-Amino-2-phenylethyl)phosphonic acid is shown to inhibit the enzymatic activity of carboxypeptidase A. Through the spectroscopic investigation of the cobalt(II) substituted enzyme we propose that it binds the enzyme in the 1:1 ratio directly at the metal, probably through the phosphate group like phosphate itself. The aromatic group is proposed to sit in the so-called S1 hydrophobic pocket. This is a unique behavior among the inhibitors of the enzyme. The S'1 site is still available in the binary adduct so that a ternary complex can be obtained with molecules like L-Phenylalanine, which enter that site.
