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Carbamoyl phosphate synthetase: a tunnel runs through it
Authors:Hazel M Holden  James B Thoden  Frank M Raushel
Institution:aDepartment of Biochemistry, University of Wisconsin, Madison, WI 53706, USA;bDepartment of Chemistry, and Department of Biochemistry and Biophysics, Texas A&;M University, College Station, TX 77843, USA
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 Å 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 Å.
Keywords:Abbreviations: CPS carbamoyl phosphate synthetase  GPATase glutamine phosphoribosylpyrophosphate amidotransferase
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