MANDELATE RACEMASE AND MUCONATE LACTONIZING ENZYME ARE MECHANISTICALLY DISTINCT AND STRUCTURALLY HOMOLOGOUS

被引:118
作者
NEIDHART, DJ
KENYON, GL
GERLT, JA
PETSKO, GA
机构
[1] MIT,DEPT CHEM,CAMBRIDGE,MA 02139
[2] UNIV CALIF SAN FRANCISCO,DEPT PHARMACEUT CHEM,SAN FRANCISCO,CA 94143
[3] UNIV MARYLAND,DEPT CHEM & BIOCHEM,COLLEGE PK,MD 20742
关键词
D O I
10.1038/347692a0
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
MANDELATE racemase (MR) and muconate lactonizing enzyme (MLE) catalyse separate and mechanistically distinct reactions necessary for the catabolism of aromatic acids by Pseudomonas putida1-3. The X-ray crystal structure of MR, solved at 2.5 Å resolution, reveals that the secondary, tertiary and quaternary structures of MR and MLE4 are remarkably similar; also, MR and MLE are about 26% identical in primary structure5. However, MR has no detectable MLE activity and vice versa. Thus, MR and MLE constitute the first example of enzymes that catalyse different reactions, as opposed to mechanistically identical reactions on different substrates, yet possess sufficient structural and sequence identity that they are likely to have evolved from a common ancestor. The discovery that MR and MLE catalyse different reactions but share a common structural framework has broad implications for the natural evolution of enzymes and metabolic pathways, as well as for the rational modification of enzyme activities. © 1990 Nature Publishing Group.
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页码:692 / 694
页数:3
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