Accepted manuscript
(+)-Larreatricin hydroxylase, an enantio-specific polyphenol oxidase from the creosote bush (Larrea tridentata)
Proceedings of the National Academy of Sciences - PNAS, Vol.100(19), pp.10641-10646
09/16/2003
Handle:
https://hdl.handle.net/2376/114168
PMCID: PMC196857
PMID: 12960376
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.
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Details
- Title
- (+)-Larreatricin hydroxylase, an enantio-specific polyphenol oxidase from the creosote bush (Larrea tridentata)
- Creators
- Man-Ho Cho - Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340, USASyed G A MoinuddinGregory L HelmsShojiro HishiyamaDietmar EichingerLaurence B DavinNorman G Lewis
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, Vol.100(19), pp.10641-10646
- Academic Unit
- Institute of Biological Chemistry; NMR Center
- Publisher
- United States
- Identifiers
- 99900547681601842
- Language
- English
- Resource Type
- Accepted manuscript