Catalytic properties of an expressed and purified higher plant type zeta-carotene desaturase from Capsicum annuum

Eur J Biochem. 1999 Oct 1;265(1):376-83. doi: 10.1046/j.1432-1327.1999.00746.x.

Abstract

The zeta-carotene desaturase from Capsicum annuum (EC 1.14.99.-) was expressed in Escherichia coli, purified and characterized biochemically. The enzyme acts as a monomer with lipophilic quinones as cofactors. Km values for the substrate zeta-carotene or the intermediate neurosporene in the two-step desaturation reaction are almost identical. Product analysis showed that different lycopene isomers are formed, including substantial amounts of the all-trans form, together with 7,7',9,9'-tetracis prolycopene via the corresponding neurosporene isomers. The application of different geometric isomers as substrates revealed that the zeta-carotene desaturase has no preference for certain isomers and that the nature of the isomers formed during catalysis depends strictly on the isomeric composition of the substrate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Capsicum / enzymology*
  • Capsicum / genetics
  • Carotenoids / metabolism*
  • Escherichia coli / genetics
  • Isomerism
  • Kinetics
  • Lycopene
  • Oxidoreductases / drug effects
  • Oxidoreductases / genetics
  • Oxidoreductases / isolation & purification
  • Oxidoreductases / metabolism*
  • Plants, Medicinal*
  • Plastoquinone / analogs & derivatives
  • Plastoquinone / pharmacology
  • Recombinant Proteins / drug effects
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Ubiquinone / analogs & derivatives
  • Ubiquinone / pharmacology

Substances

  • Recombinant Proteins
  • decylplastoquinone
  • Ubiquinone
  • Carotenoids
  • neurosporene
  • 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
  • Oxidoreductases
  • zeta-carotene desaturase
  • Plastoquinone
  • Lycopene

Associated data

  • GENBANK/X89897