A mechanism of L-canaline toxicity.
L-Canaline, a highly toxic structural analogue of L-ornithine, reacted with pyridoxal phosphate to form a stable, ninhydrin-positive complex. NMR analysis revealed the involvement of a Schiff's base in complex formation. Interaction of L-canaline with L-tyrosine decarboxylase, a known B6-containing enzyme, curtailed significantly enzyme-mediated decarboxylation. Spectral scans provided evidence that the loss in catalytic activity is associated with the reaction of canaline with the pyridoxal phosphate moiety of the enzyme. Thus, the marked antimetabolic properties of canaline are due in part of its ability to form a Schiff's-base-containing complex with the B6 moiety of the enzyme.
D000613:Aminobutyrates / Q000494:pharmacology / Q000633:toxicity*; D000818:Animals; D001681:Biological Assay; D009682:Magnetic Resonance Spectroscopy; D011732:Pyridoxal Phosphate / Q000494:pharmacology; D013053:Spectrophotometry; D014445:Tyrosine Decarboxylase / Q000378:metabolism
D000613:Aminobutyrates; C001926:canaline; D011732:Pyridoxal Phosphate; D014445:Tyrosine Decarboxylase