THE UNUSUAL BEHAVIOR OF THE INHIBITOR S(+)(1-AMINO-2-PHENYLETHYL)PHOSPHONIC ACID TOWARDS CARBOXYPEPTIDASE-A

被引:17
作者
BAL, W
BERTINI, I
KOZLOWSKI, H
MONNANNI, R
SCOZZAFAVA, A
SIATECKI, GZ
机构
[1] UNIV FLORENCE,DEPT CHEM,VIA G CAPPONI 7,I-50121 FLORENCE,ITALY
[2] WROCLAW B BEIRUT UNIV,INST CHEM,PL-50137 WROCLAW,POLAND
关键词
D O I
10.1016/0162-0134(90)80056-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The molecule (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. © 1990.
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页码:227 / 235
页数:9
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