Carbon 13 NMR study of nonenzymatic reactions of pyridoxal 5'-phosphate with selected amino acids and of related reactions.
Carbon 13 nuclear magnetic resonance spectroscopy has been used to monitor the nonenzymatic reactions of pyridoxal 5'-phosphate with glycine, alanine, valine, serine, and with several other model compounds. Isotopically enriched amino acids were employed so that low concentrations could be utilized while still allowing relatively rapid acquisition of spectral data. The results for alanine and serine are particularly noteworthy in that alanine is deaminated to pyruvate and pyruvate is aminated to alanine, but contrary to the enzymatic reactions of various serine dehydratases wherein serine is converted to pyruvate, the nonenzymatic reaction utilizing serine results in hydroxypruvate rather than pyruvate formation. In the reverse reaction, hydroxypyruvate is aminated to serine but very inefficiently relative to the amination of pyruvate to alanine. The experimental results have been formulated into a proposed reaction mechanism for deamination of amino acids by pyridoxal-P.
D000409:Alanine; D000596:Amino Acids; D000641:Ammonia; D001665:Binding Sites; D002247:Carbon Isotopes; D055598:Chemical Phenomena; D002621:Chemistry; D005557:Formaldehyde; D005998:Glycine; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D011732:Pyridoxal Phosphate; D011733:Pyridoxamine; D012521:Sarcosine; D013329:Structure-Activity Relationship
D000596:Amino Acids; D002247:Carbon Isotopes; D005557:Formaldehyde; D011732:Pyridoxal Phosphate; D011733:Pyridoxamine; D000641:Ammonia; D000409:Alanine; D005998:Glycine; D012521:Sarcosine