MUTAGENESIS AND LAUE STRUCTURES OF ENZYME INTERMEDIATES - ISOCITRATE DEHYDROGENASE

被引：116

作者：

BOLDUC, JM

DYER, DH

SCOTT, WG

SINGER, P

SWEET, RM

KOSHLAND, DE

STODDARD, BL

机构：

[1] MRC, MOLEC BIOL LAB, CAMBRIDGE CB2 2QH, ENGLAND

[2] BROOKHAVEN NATL LABS, DEPT BIOL STRUCT, UPTON, NY 11973 USA

[3] UNIV CALIF BERKELEY, DEPT MOLEC & CELL BIOL, BERKELEY, CA 94720 USA

来源：

SCIENCE | 1995年 / 268卷 / 5215期

关键词：

D O I：

10.1126/science.7761851

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：

Site-directed mutagenesis and Laue diffraction data to 2.5 Angstrom resolution were used to solve the structures of two sequential intermediates formed during the catalytic actions of isocitrate dehydrogenase. Both intermediates are distinct from the enzyme-substrate and enzyme-product complexes. Mutation of key catalytic residues changed the rate determining steps so that protein and substrate intermediates within the overall reaction pathway could be visualized.

引用

页码：1312 / 1318

页数：7

共 24 条

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