, Volume 214, Issue 5, pp 727–733

Benzoic acid biosynthesis in cell cultures of Hypericum androsaemum

  • Ahmed M. Abd El-Mawla
  • Ludger Beerhues
Original Article

DOI: 10.1007/s004250100657

Cite this article as:
Abd El-Mawla, A.M. & Beerhues, L. Planta (2002) 214: 727. doi:10.1007/s004250100657


Biosynthesis of benzoic acid from cinnamic acid has been studied in cell cultures of Hypericum androsaemum L. The mechanism underlying side-chain shortening is CoA-dependent and non-β-oxidative. The enzymes involved are cinnamate:CoA ligase, cinnamoyl-CoA hydratase/lyase and benzaldehyde dehydrogenase. Cinnamate:CoA ligase was separated from benzoate:CoA ligase and 4-coumarate:CoA ligase, which belong to xanthone biosynthesis and general phenylpropanoid metabolism, respectively. Cinnamoyl-CoA hydratase/lyase catalyzes hydration and cleavage of cinnamoyl-CoA to benzaldehyde and acetyl-CoA. Benzaldehyde dehydrogenase finally supplies benzoic acid. In cell cultures of H. androsaemum, benzoic acid is a precursor of xanthones, which accumulate during cell culture growth and after methyl jasmonate treatment. Both the constitutive and the induced accumulations of xanthones were preceded by increases in the activities of all benzoic acid biosynthetic enzymes. Similar changes in activity were observed for phenylalanine ammonia-lyase and the xanthone biosynthetic enzymes benzoate:CoA ligase and benzophenone synthase.

Benzaldehyde dehydrogenase Benzoic acid biosynthesis Cinnamate:CoA ligase Cinnamoyl-CoA hydratase/lyase Hypericum (cell culture) Xanthone biosynthesis

Copyright information

© Springer-Verlag 2001

Authors and Affiliations

  • Ahmed M. Abd El-Mawla
    • 1
  • Ludger Beerhues
    • 1
  1. 1.Institut für Pharmazeutische Biologie, Mendelssohnstraβe 1, 38106 Braunschweig, Germany
  2. 2.Present address: Department of Pharmacognosy, Faculty of Pharmacy, Assiut University, Assiut 71526, Egypt