Enzymatic formation of unnatural novel polyketides from alternate starter and nonphysiological extension substrate by chalcone synthase.
[reaction: see text] In the chalcone synthase (CHS) enzyme reaction, both the starter molecule and the extension unit of the polyketide chain elongation reaction were simultaneously replaced with nonphysiological substrates. When incubated with benzoyl-CoA and methylmalonyl-CoA as substrates, recombinant CHS from Scutellaria baicalensis afforded an unnatural novel triketide, 4-hydroxy-3,5-dimethyl-6-phenyl-pyran-2-one, along with a tetraketide, 4-hydroxy-3,5-dimethyl-6-(1-methyl-2-oxo-2-phenyl-ethyl)-pyran-2-one. On the other hand, the enzyme also accepted hexanoyl-CoA and methylmalonyl-CoA as substrates to produce an unnatural novel triketide, 4-hydroxy-3,5-dimethyl-6-pentyl-pyran-2-one.
Abe
Ikuro
I
University of Shizuoka, School of Pharmaceutical Sciences, and The 21st Century COE Program, 52-1 Yada, Shizuoka 422-8526, Japan. abei@ys7.u-shizuoka-ken.ac.jp
Takahashi
Yusuke
Y
Lou
Weiwei
W
Noguchi
Hiroshi
H
D000214:Acyl Coenzyme A / Q000378:metabolism; D000217:Acyltransferases / Q000737:chemistry / Q000378:metabolism*; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism; D011753:Pyrones / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D031364:Scutellaria baicalensis / Q000201:enzymology
D000214:Acyl Coenzyme A; D010940:Plant Proteins; D011753:Pyrones; D011994:Recombinant Proteins; C015357:methylmalonyl-coenzyme A; C037817:benzoyl-coenzyme A; D000217:Acyltransferases; C020141:flavanone synthetase