Carbamoyl phosphate synthetase: a tunnel runs through it

被引：37

作者：

Holden, HM ^{[1
]}

Thoden, JB

Raushel, FM

机构：

[1] Univ Wisconsin, Dept Biochem, Madison, WI 53706 USA

[2] Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA

[3] Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1998年 / 8卷 / 06期

关键词：

D O I：

10.1016/S0959-440X(98)80086-9

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 direct transfer of metabolites from one protein to another in a biochemical pathway or between one active site and another within a single enzyme has been described as substrate channeling. The first structural Visualization of such a phenomenon was provided by the X-ray crystallographic analysis of tryptophan synthase, in which a tunnel of approximately 25 Angstrom in length was observed. The recently determined three-dimensional structure of carbamoyl phosphate synthetase sets a new long distance record in that the three active sites are separated by nearly 100 Angstrom.

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页码：679 / 685

页数：7

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