SEQUENCE, STRUCTURE AND ACTIVITY OF PHOSPHOGLYCERATE KINASE - POSSIBLE HINGE-BENDING ENZYME

被引：470

作者：

BANKS, RD ^{[1
]}

BLAKE, CCF ^{[1
]}

EVANS, PR ^{[1
]}

HASER, R ^{[1
]}

RICE, DW ^{[1
]}

HARDY, GW ^{[1
]}

MERRETT, M ^{[1
]}

PHILLIPS, AW ^{[1
]}

机构：

[1] WELLCOME RES LABS, DEPT PROT CHEM, BECKENHAM BR3 3BS, KENT, ENGLAND

来源：

NATURE | 1979年 / 279卷 / 5716期

关键词：

D O I：

10.1038/279773a0

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：

The fitting of sequenced peptides to a high-resolution X-ray map of phosphoglycerate kinase [EC 2.7.2.3] has yielded the complete sequence and structure of the horse muscle enzyme. Metal ADP and ATP substrates are bound to 1 of the 2 widely separated domains in an environment that seems unsuitable for phosphoglycerate binding. The most plausible binding site for the phosphoglycerate substrate is on the other domain about 10 .ANG. from the ATP, which implies the possibility of a large scale hinge-bending of the domains to bring the 2 substrates together in a water-free environment for catalysis.

引用

页码：773 / 778

页数：6

共 27 条

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