Deuterium isotope effect in enzymatic transamination of L-deuterio-phenylalanine to deuterio-phenylpyruvic acid

✍ Scribed by H. J. Rhodes; R. B. Kluza; M. I. Blake

• Publisher: John Wiley and Sons
• Year: 1973
• Tongue: English
• Weight: 617 KB
• Volume: 62
• Category: Article
• ISSN: 0022-3549
• DOI: 10.1002/jps.2600620110

✦ Synopsis

L-Deuterio-phenylalanine was isolated by gradient elution ion-exchange chromatography of the ionic fraction obtained from the cell wall hydrolysate of algae grown in culture medium containing 9 9 . 6 z deuterium oxide. The enzyme system present in rat brain extract was used for determining the rate of transamination of L-deuterio-phenylalanine and its protio analog.

The phenylpyruvate formed was determined spectrophotometrically at 300 nm. using the arsenate-catalyzed enol-borate assay procedure. Transamination rates were determined in media containing varying concentrations of amino acid and m-ketoglutarate. Kinetic determination of maximum velocity was conducted through graphical analysis of the data. The deuterium isotope effect, expressed as the V H / V D value, was 1.64.

Keyphrases [7 L-Deuterio-and L-protio-phenylalanine-isolation, identification, enzyme transamination to phenylpyruvates, deuterium isotope effect 0 Deuterio-phenylpyruvic acid-enzymatic transamination product from L-deuterio-phenylalanine, deuterium isotopc effect 0 Deuterium isotope effect-L-deuterio-phenylalanine enzyme transamination to deuterio-phenylpyruvic acid 0

Transamination rates-L-deuterio-and L-protio-phenylalanine, deuterium isotope effect 0 Ion-exchange chromatography-isolation, L-dcuterio-phenylalanine 0 UV spectrophotometry-monitoring, L-deuterio-phenylalanine transamination