title: Pyruvate carboxylase: affinity labelling of the magnesium adenosine triphosphate binding site.
abstract: The 2' , 3'-dialdehyde derivative of ATP (oATP) was prepared by periodate oxidation and on the following criteria was considered to be an effective affinity label.  The magnesium complex of this derivative (Mg-oATP2) was shown to ba linear competitive inhibitor with respect to MgATP2-in both the acetyl-CoA-dependent and -independent activities of the enzyme but was a non-competitive inhibitor with respect to bicarbonate, and an uncompetitive inhibitor with respect to pyruvate.  Mg-oATP was covalently bound to pyruvate carboxylase by reduction using sodium borohydride with concurrent irreversible inactivation of the enzyme...
mesh_terms: D000105:Acetyl Coenzyme A / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000345:Affinity Labels; D000818:Animals; D001665:Binding Sites; D007700:Kinetics; D008239:Lysine / Q000032:analysis; D008274:Magnesium / Q000494:pharmacology*; D008930:Mitochondria, Liver / Q000201:enzymology; D011485:Protein Binding; D011766:Pyruvate Carboxylase / Q000378:metabolism*; D012756:Sheep
chemical_list: D000345:Affinity Labels; D000105:Acetyl Coenzyme A; D000255:Adenosine Triphosphate; D011766:Pyruvate Carboxylase; D008274:Magnesium; D008239:Lysine