ANTIBODY CATALYSIS OF PEPTIDE-BOND FORMATION

被引：46

作者：

JACOBSEN, JR ^{[1
]}

SCHULTZ, PG ^{[1
]}

机构：

[1] UNIV CALIF BERKELEY,DEPT CHEM,BERKELEY,CA 94720

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1994年 / 91卷 / 13期

关键词：

D O I：

10.1073/pnas.91.13.5888

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

An antibody generated against a neutral phosphonate diester transition-state (TSdouble dagger) analog catalyzes the formation of an amide bond between a phenylalanyl amino group and an acyl azide derived from L-alanine. The antibody is selective for L- vs. D-alanine and does not catalyze the hydrolysis of the acyl azide to an appreciable degree. A rate acceleration of 10,000-fold relative to the uncatalyzed reaction is observed. The antibody may achieve its catalytic efficiency both by acting as an entropy trap and by stabilizing the deprotonated form of the amine nucleophile. These experiments constitute a first step toward a general strategy for the generation of sequence-specific peptide ligases.

引用

页码：5888 / 5892

页数：5

共 17 条

[1] ENGINEERING SUBTILISIN AND ITS SUBSTRATES FOR EFFICIENT LIGATION OF PEPTIDE-BONDS IN AQUEOUS-SOLUTION [J].