Phlorisovalerophenone synthase, a novel polyketide synthase from hop (Humulus lupulus L.) cones.
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.
Paniego
N B
NB
Divison of Pharmacognoxy, Leiden/Amsterdam Center for Drug Research, Gorlaeus Laboratories, Leiden, The Netherlands.
Zuurbier
K W
KW
Fung
S Y
SY
van der Heijden
R
R
Scheffer
J J
JJ
Verpoorte
R
R
D000217:Acyltransferases / Q000737:chemistry / Q000302:isolation & purification; D000595:Amino Acid Sequence; D002384:Catalysis; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D019685:Rosales / Q000201:enzymology*
D000217:Acyltransferases; C119535:phlorisovalerophenone synthase