Journal
BIOORGANIC & MEDICINAL CHEMISTRY
Volume 16, Issue 17, Pages 8117-8126Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2008.07.052
Keywords
enzyme catalysis; prenylation; flavonoid; polyketide; kinetics
Funding
- METI
- MEXT, Japan [18018008]
- HHMI
- Grants-in-Aid for Scientific Research [18018008] Funding Source: KAKEN
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NphB is a soluble prenyltransferase from Streptomyces sp. strain CL190 that attaches a geranyl group to a 1,3,6,8-tetrahydroxynaphthalene-derived polyketide during the biosynthesis of anti-oxidant naphterpin. Here we report multiple chemoenzymatic syntheses of various prenylated compounds from aromatic substrates including flavonoids using two prenyltransferases NphB and SCO7190, a NphB homolog from Streptomyces coelicolor A3( 2), as biocatalysts. NphB catalyzes carbon-carbon-based and carbon-oxygen-based geranylation of a diverse collection of hydroxyl-containing aromatic acceptors. Thus, this simple method using the prenyltransferases can be used to explore novel prenylated aromatic compounds with biological activities. Kinetic studies with NphB reveal that the prenylation reaction follows a sequential ordered mechanism. (C) 2008 Elsevier Ltd. All rights reserved.
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