Zeitschrift für Naturforschung 49c: 781-790 (1994)

Phenylalanine analogues: Potent inhibitors of phenylalanine ammonia-lyase are weak inhibitors of phenylalanine-tRNA synthetases

Gerhard Leubner-Metzger and Nikolaus Amrhein

Hyperlink to: Appert, Zon, Amrhein (2003) Phytochemistry 62: 415-422
Kinetic analysis of the inhibition of phenylalanine ammonia-lyase by 2-aminoindan-2-phosphonic acid and other phenylalanine analogues

Tab. 2 PRS

Table II. Km values of the PRS from wheat germ (Triticum aestivum), soybean cotyledons (Glycine max), and baker's yeast (Saccharomyces cerevisiae). Apparent Km values for the different substrates in the tRNA-phe aminoacylation and the ATP-PPi exchange assays were determined for the enzymes from the three sources at pH 8.2, 7.8, and 7.4 respectively.

Article in PDF format (4.4 MB)           Abstract          Fig. 1          Fig. 2          Tab. 1          Tab. 2          Tab. 3          Tab. 4          Phe-analogues  

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