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Carbamoyl phosphate synthetase: a tunnel runs through it.
Holden, H M; Thoden, J B; Raushel, F M.
Affiliation
  • Holden HM; Department of Biochemistry University of Wisconsin Madison WI 53706 USA. holden@enzyme.wisc.edu
Curr Opin Struct Biol ; 8(6): 679-85, 1998 Dec.
Article in En | MEDLINE | ID: mdl-9914247
ABSTRACT
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 A 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 A.
Subject(s)
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Database: MEDLINE Main subject: Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) Language: En Year: 1998 Type: Article
Search on Google
Database: MEDLINE Main subject: Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) Language: En Year: 1998 Type: Article