Phosphopyridoxal complexes with histamine and histidine. (4) The kinetics of complex formation between histidine and pyridoxal 5' -phosphate in the presence of bacterial histidine decarboxylase.
The dynamics of the complex formation between pyridoxal 5'-phosphate (PLP) and histidine in the presence of bacterial histidine decarboxylase was examined. Since PLP is able to form a cyclic product with histidine and histamine, the possibility of complex formation between PLP and histamine formed during a decarboxylation reaction was examined too. It was found that the cyclization reaction between PLP and histidine is equimolecular and the rate of cyclic product formation is not significantly influenced by the presence of enzyme. In the presence of bacterial histidine decarboxylase both the cyclization reaction and cyclic product formation were observed. Predominance of histamine or cyclic product formation was dependent on pH and substrate concentration. In the presence of histidine and enzymatic protein, histamine formed during the decarboxylation reaction was unable to form a cyclic product with PLP.
D002262:Carboxy-Lyases / Q000378:metabolism*; D003016:Clostridium perfringens / Q000201:enzymology; D006639:Histidine / Q000378:metabolism*; D006640:Histidine Decarboxylase / Q000378:metabolism*; D007700:Kinetics; D011732:Pyridoxal Phosphate / Q000378:metabolism*
D006639:Histidine; D011732:Pyridoxal Phosphate; D002262:Carboxy-Lyases; D006640:Histidine Decarboxylase