Mechanistic Investigation of Phenylalanine Ammonia Lyase by Using N-Methylated Phenylalanines

Sandra Viergutz, László Poppe, Anna Tomin, János Rétey

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

N-Methyl-L-phenylalanine (5), N-methyl-4-nitro-L-phenylalanine (6), and N,N-dimethyl-4-nitro-L-phenyl-alanine (7·H+) were investigated as substrates of inhibitors of phenylalanine ammonia lyase from Petroselinum crispum. Whereas the former was a reluctant substrate (K m = 6.6 mM, kcat = 0.22 s-1), no reverse reaction could be detected by using methylamine and (E)-cinnamate (2). The Km value for ammonia in the reverse reaction by using (E)-cinnamate (2) was determined to be 4.4 and 2.6M at pH 8.8 and 10, respectively. The N-methylated 4-nitro-L-phenylalanines 6 and 7 showed only strong inhibitory effects (Ki = 130 nM and 8 nM, resp.). These and former results are discussed in terms of the mechanism of action of phenyalalanine and histidine ammonia lyases.

Original languageEnglish
Pages (from-to)3601-3612
Number of pages12
JournalHelvetica Chimica Acta
Volume86
Issue number11
DOIs
Publication statusPublished - Dec 29 2003

ASJC Scopus subject areas

  • Catalysis
  • Biochemistry
  • Drug Discovery
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

Fingerprint Dive into the research topics of 'Mechanistic Investigation of Phenylalanine Ammonia Lyase by Using N-Methylated Phenylalanines'. Together they form a unique fingerprint.

  • Cite this