Fujioka T, Tanizawa K, Kanaoka Y
J Biochem. 1981 Feb;89(2):637-43. doi: 10.1093/oxfordjournals.jbchem.a133240.
p-Amidinophenyl esters derived from a variety of amino acids and peptides, including D-amino acids, were synthesized. The kinetic behavior of trypsin towards these esters, which are "inverse substrates," was analyzed. Deacylation rates of acyl trypsins carrying D-amino acid residues were determined for the first time by the use of these "inverse substrates." The steric requirements of the catalytic site region of trypsin were successfully analyzed by studying the deacylation process as manifested in the hydrolyses of enatiomeric pairs of "inverse substrates." The effects of chiral ligands on the deacylation process were also studied in connection with the chiral requirements of the active site.
合成了源自多种氨基酸和肽（包括D-氨基酸）的对脒基苯酯。分析了胰蛋白酶对这些作为“反向底物”的酯的动力学行为。首次通过使用这些“反向底物”测定了携带D-氨基酸残基的酰基胰蛋白酶的脱酰化速率。通过研究对映体对“反向底物”水解中表现出的脱酰化过程，成功分析了胰蛋白酶催化位点区域的空间要求。还结合活性位点的手性要求研究了手性配体对脱酰化过程的影响。
