Carbamoyl phosphate synthetase: a tunnel runs through it. Academic Article

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.

authors

• Raushel, Frank

published proceedings

• Curr Opin Struct Biol

altmetric score

• 3

author list (cited authors)

• Holden, H. M., Thoden, J. B., & Raushel, F. M.

citation count

• 40

complete list of authors

• Holden, HM||Thoden, JB||Raushel, FM

publication date

• January 1998

publisher

• Elsevier  Publisher

published in

• Current Opinion in Structural Biology  Journal

keywords

• Binding Sites
• Biopolymers
• Carbamoyl-phosphate Synthase (glutamine-hydrolyzing)
• Crystallography, X-Ray
• Protein Conformation

Digital Object Identifier (DOI)

• 10.1016/s0959-440x(98)80086-9

start page

• 679

end page

• 685

volume

• 8

issue

• 6

URL

• http://dx.doi.org/10.1016/s0959-440x(98)80086-9