作者:Tohru Takarada、Morio Yashiro、Makoto Komiyama
DOI:10.1002/1521-3765(20001103)6:21<3906::aid-chem3906>3.3.co;2-a
日期:2000.11.3
Oligopeptides are efficiently hydrolyzed by Ce-IV to the corresponding amino acids under mild conditions. The pseudo first-order rate constants for the hydrolysis of H-Gly-Phe-OH and H-Gly-Gly-OH at pH 7.0 and 50 degreesC are 3.5 x 10(-1) and 2.8 x 10(-1) h(-1), with [Ce(NH4)(2)(NO3)(6)](0) 10mM (the half-lives are 2.0 and 2.5 h). The catalytic activity of the Ce-IV is far greater than those of other lanthanide ions and non-lanthanide ions. No oxidative cleavage was observed under the reaction conditions. Catalytic turnover of the Ce-IV was also evidenced. The hydrolysis is fast especially when the substrates have no metal-coordinating side chains. Tripeptides and tetrapeptides are hydrolyzed at the similar rates as the dipeptides. In the hydrolysis of tripeptides, the amide linkage near the N-terminus is preferentially hydrolyzed. Neither the N-carbobenzploxy derivative nor the amide of H-Gly-Phe-OH is hydrolyzed to a measurable extent, showing that both the terminal amino group and the carboxylate are coordinated to the Ce-IV ion. This complexation is further confirmed by H-1 NR-IR spectroscopy. The Ce-IV ion is therefore one of the most active catalysts for peptide hydrolysis.