pyruvoyl-dependent decarboxylase, synthesised as zymogen. The pyruvoyl cofactor results from the self-modification of an internal serine (Ser82) residue of the proenzyme, the pyruvoyl group functions through the formation of a Schiff base with the substrate to promote decarboxylation
PLP, the cofactor binding at the active site induces conformational changes in the enzyme, pyridoxal 5'-phosphate binding is important for substrate binding, the substrate might bind to ADC only after PLP binding
the pyruvoyl group of the enzyme is generated by an autocatalytic internal serinolysis reaction at Ser53 in the proenzyme resulting in two polypeptide chains
the pyruvoyl group of the enzyme is generated by an autocatalytic internal serinolysis reaction at Ser53 in the proenzyme resulting in two polypeptide chains
the enzyme contains a reactive pyruvoyl group, the proenzyme undergoes autocatalytic serinolysis, resulting in the formation of two chains and the creation of a pyruvoyl group, which is the cofactor for the decarboxylation reaction
the enzyme contains a reactive pyruvoyl group, the proenzyme undergoes autocatalytic serinolysis, resulting in the formation of two chains and the creation of a pyruvoyl group, which is the cofactor for the decarboxylation reaction
pyruvoyl-dependent decarboxylase, synthesised as zymogen. The pyruvoyl cofactor results from the self-modification of an internal serine (Ser44) residue of the proenzyme, the pyruvoyl group functions through the formation of a Schiff base with the substrate to promote decarboxylation
pyruvoyl-dependent decarboxylase, synthesised as zymogen. The pyruvoyl cofactor results from the self-modification of an internal serine (Ser44) residue of the proenzyme, the pyruvoyl group functions through the formation of a Schiff base with the substrate to promote decarboxylation