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Mechanistic Insights into Carbamoyl Phosphate Synthetase with Adaptive Linker Variants

This study explores the enzymatic behavior of Carbamoyl Phosphate Synthetase (CPS) through the investigation of wild-type and DAD (DA linker) variants. The focus lies on the interaction between substrates such as ATP, bicarbonate, and aspartate, alongside the effects of exogenous "cold" carbamoyl phosphate. The research highlights observed vs. theoretical concentrations in various conditions, emphasizing the distinct channeling of carbamoyl phosphate in wild-type CPS compared to the non-channeling DAD variant. Insights are adapted from key biochemical literature, enhancing our understanding of CPS mechanisms.

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Mechanistic Insights into Carbamoyl Phosphate Synthetase with Adaptive Linker Variants

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  1. 0 0.25 0.5 0.75 1 CPS ATCase 14Carbamoyl Aspartate 14Carbamoyl Phosphate H14CO3- Gln, H2O, ATP Asp “cold” Carbamoyl Aspartate “Cold” Carbamoyl Phosphate DA Linker DHO ATCase CP Sase Wild-Type C N CP Sase ATCase DHO Without DA Linker (DAD) N C Wild-type DAD 5 5 4 4 14Carbamoyl Aspartate (mM) 3 3 Observed ( ) Theoretical ( ) 2 2 Observed ( ) 1 1 Theoretical ( ) 0 0.25 0.5 0.75 1 Exogenous (“cold” )Carbamoyl Phosphate (mM) GLU GLU DHO DHO DA Linker GLN GLN NH3 NH3 CAsp CAsp HCO3- HCO3- CAsp CBX CBM CBX CBM CAsp CP CP ATP ATP CP CP CP ASP ATP ATP ASP Channeling of CP(Wild-type) No Channeling of CP(DAD) Adapted from Guy&Evans, J.Biol.Chem (1994), V269:23808-16

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