The 5'-O-phosphonomethyl analog of ATP. Studies of substrate properties in ligase-dependent reactions.
The 5-O-phosphonomethyl analog of ATP (ATPc) and its interaction with different enzymes, catalysing synthesis of C-O-, C-S-, C-N- and C-C-bond were investigated. It was shown ATPc to have substrate properties and to be involved in all studied ligase-dependent reactions. Kinetic parameters of the interaction of alternative substrate - ATPc with all studied enzymes were established and the comparison of ATPc with other phosphonate analogs of ATP was performed.
D000103:Acetyl-CoA Carboxylase / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000138:chemical synthesis*; D001217:Aspartate-Ammonia Ligase / Q000378:metabolism; D007700:Kinetics; D008025:Ligases / Q000378:metabolism*; D063065:Organophosphonates; D010652:Phenylalanine-tRNA Ligase / Q000378:metabolism; D013379:Substrate Specificity; D014637:Valine-tRNA Ligase / Q000378:metabolism
D063065:Organophosphonates; D000255:Adenosine Triphosphate; D008025:Ligases; D010652:Phenylalanine-tRNA Ligase; D014637:Valine-tRNA Ligase; D001217:Aspartate-Ammonia Ligase; D000103:Acetyl-CoA Carboxylase