Phenylalanine ammonia-lyase: enzymic conversion of 3-(1,4-cyclohexadienyl)-L-alanine to trans-3-(1,4-cyclohexadienyl)acrylic acid

• Published in: Biochemistry (Easton) Vol. 18; no. 8; pp. 1431 - 1438
• Main Authors: Hanson, Kenneth R, Havir, Evelyn A, Ressler, Charlotte
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 17.04.1979
• Subjects: Acrylates - metabolism; Alanine - analogs & derivatives; Alanine - metabolism; Ammonia-Lyases - metabolism; Kinetics; Phenylalanine Ammonia-Lyase - metabolism; Plants - enzymology; Rhodotorula - enzymology; Spectrophotometry, Ultraviolet
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi00575a007

The phenylalanine analogue 3-(1,4-cyclohexadienyl)-L-alanine is converted to the hitherto unknown cinnamate analogue trans-3-(1,4-cyclohexadienyl)acrylic acid by L-phenylalanine ammonia-lyase (EC 4.3.1.5) from maize, potato, or Rhodotorula glutinis. The structure assigned to the product is confirmed by its 1H nuclear magnetic resonance spectrum and by the chemical synthesis to be described in a subsequent paper. On comparing the above substrate analogue with L-phenylalanine, the Km was lowered only slightly but kcat was reduced 14--40-fold depending on the source of the enzyme. Because the compounds closely resemble each other in size and hydrophobic properties, this lowering of kcat may be attributed to the electronic effect of replacing the pi electrons of the aromatic system by those of a double bond. Correct alignment at the active site appears to depend upon the space-filling properties of the ring system; open chain analogues that retain the gamma, beta double bond were found to be inhibitors, not substrates.