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- Title
Phlorisovalerophenone synthase, a novel polyketide synthase from hop (Humulus lupulus L.) cones.
- Authors
Paniego, N B; Zuurbier, K W; Fung, S Y; van der Heijden, R; Scheffer, J J; Verpoorte, R
- Abstract
Phlorisovalerophenone synthase (VPS), a novel aromatic polyketide synthase, was purified to homogeneity from 4.2 mg protein extract obtained from hop (Humulus lupulus L.) cone glandular hairs. The enzyme uses isovaleryl-CoA or isobutyryl-CoA and three molecules of malonyl-CoA to form phlorisovalerophenone or phlorisobutyrophenone, intermediates in the biosynthesis of the hop bitter acids (alpha- and beta-acids). VPS is an homodimeric enzyme, with subunits of 45 kDa. The pI of the enzyme was 6.1. Km values of 4 microm for isovaleryl-CoA, 10 microm for isobutyryl-CoA and 33 microm for malonyl-CoA, were found. The amino-acid sequences of two peptides, obtained by digestion of VPS, showed that the enzyme is highly homologous to plant chalcone synthases. The functional and structural relationship between VPS and other aromatic polyketide synthases is discussed.
- Publication
European journal of biochemistry, 1999, Vol 262, Issue 2, p612
- ISSN
0014-2956
- Publication type
Journal Article
- DOI
10.1046/j.1432-1327.1999.00444.x