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Updated: Aug 15, 2026

Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System
Published on: August 1, 2016
Abstract:
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.
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