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  • Chemoenzymatic syntheses of prenylated aromatic small molecules using Streptomyces prenyltransferases with relaxed substrate specificities.

Chemoenzymatic syntheses of prenylated aromatic small molecules using Streptomyces prenyltransferases with relaxed substrate specificities.

Bioorganic & medicinal chemistry (2008-08-07)
Takuto Kumano, Stéphane B Richard, Joseph P Noel, Makoto Nishiyama, Tomohisa Kuzuyama
ABSTRACT

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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Genistein, from Glycine max (soybean), ~98% (HPLC)
Sigma-Aldrich
Apigenin, ≥95.0% (HPLC)
Sigma-Aldrich
1,6-Dihydroxynaphthalene, 99%
Sigma-Aldrich
Genistein, synthetic, ≥98% (HPLC), powder
Supelco
Resveratrol, analytical standard
Sigma-Aldrich
2,7-Dihydroxynaphthalene, 97%
Sigma-Aldrich
Resveratrol, ≥99% (HPLC)
Sigma-Aldrich
Daidzein, ≥98%, synthetic