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Structure and Function of Carbamoyl Phosphate Synthetase: Insights into Enzyme Catalysis

This study explores the three catalytic domains and a tunnel in the carbamoyl phosphate synthetase, highlighting the role of glutaminase and carboxy phosphate synthetase. The interactions between glutamine and water to produce carbamoyl phosphate are analyzed, with specific focus on half-lives (t1/2) and the spatial arrangement of active sites. Insights are drawn from the structural organization of the enzyme, demonstrating the separation of active sites and their distinct functions in the catalytic process.

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Structure and Function of Carbamoyl Phosphate Synthetase: Insights into Enzyme Catalysis

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  1. HO C= O O-PO32- : : NH3 NH3 O -O C= O ADP-O-P-O- NH2 -O O 2-3OP- C= O O-NH2 Three catalytic domains and a tunnel in the carbamoyl phosphate synthetase Glutaminase Carboxy Phosphate Synthetase Glutamine + H2O Carboxy Phosphate (t1/2 = 70 ms) HO C= Glutamate O -O O ADP-O-P-O- Carbamate (t1/2 = 28 ms) -O Carbamoyl Phosphate synthetase + ADP Carbamoyl Phosphate The 3 active sites are separated by 100 A Magenta = glutaminase Green = Carboxy phosphate synthetase Blue = Carbamoyl phosphate synthetase From Curr Opin Struct Biol. 1998 (6):679-85

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