(+)-Larreatricin hydroxylase, an enantio-specific polyphenol oxidase from the creosote bush (Larrea tridentata)

Proc Natl Acad Sci U S A. 2003 Sep 16;100(19):10641-6. doi: 10.1073/pnas.1934562100. Epub 2003 Sep 5.

Abstract

An enantio-specific polyphenol oxidase (PPO) was purified approximately 1,700-fold to apparent homogeneity from the creosote bush (Larrea tridentata), and its encoding gene was cloned. The posttranslationally processed PPO ( approximately 43 kDa) has a central role in the biosynthesis of the creosote bush 8-8' linked lignans, whose representatives, such as nordihydroguaiaretic acid and its congeners, have potent antiviral, anticancer, and antioxidant properties. The PPO primarily engenders the enantio-specific conversion of (+)-larreatricin into (+)-3'-hydroxylarreatricin, with the regiochemistry of catalysis being unambiguously established by different NMR spectroscopic analyses; the corresponding (-)-enantiomer did not serve as a substrate. This enantio-specificity for a PPO, a representative of a widespread class of enzymes, provides additional insight into their actual physiological roles that hitherto have been difficult to determine.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Catechol Oxidase / chemistry
  • Catechol Oxidase / genetics
  • Catechol Oxidase / metabolism*
  • Cloning, Molecular
  • DNA, Complementary
  • Larrea / enzymology*
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid
  • Stereoisomerism

Substances

  • DNA, Complementary
  • (+)-Larreatricin hydroxylase, creosote bush
  • Catechol Oxidase

Associated data

  • GENBANK/AY370019