TAILIEUCHUNG - Báo cáo khoa học: An acridone-producing novel multifunctional type III polyketide synthase from Huperzia serrata

A cDNA encoding a novel plant type III polyketide synthase was cloned and sequenced from the Chinese club moss Huperzia serrata(Huperzia-ceae). The deduced amino acid sequence ofHu. serratapolyketide synthase 1 showed 44–66% identity to those of other chalcone synthase superfamily enzymes of plant origin. | ỊFEBS Journal An acridone-producing novel multifunctional type III polyketide synthase from Huperzia serrata Kiyofumi Wanibuchi1 Ping Zhang1 2 Tsuyoshi Abe1 Hiroyuki Morita3 Toshiyuki Kohno3 Guoshen Chen2 Hiroshi Noguchi1 and Ikuro Abe1 4 1 Schoolof PharmaceuticalSciences and the COE 21 Program University of Shizuoka Japan 2 Institute of Materia Medica Zhejiang Academy of MedicalSciences Hangzhou Zhejiang China 3 Mitsubishi Kagaku Institute of Life Sciences MITILS Machida Tokyo Japan 4 PRESTO Japan Science and Technology Agency Kawaguchi Saitama Japan Keywords acridone chalcone synthase Huperzia serrata type III polyketide synthase Correspondence I. Abe University of Shizuoka 52-1 Yada Shizuoka 422-8526 Japan Fax Tel 81 54 264 5662 E-mail abei@ Received 30 October 2006 revised 15 December 2006 accepted 19 December 2006 doi A cDNA encoding a novel plant type III polyketide synthase was cloned and sequenced from the Chinese club moss Huperzia serrata Huperzia-ceae . The deduced amino acid sequence of Hu. serrata polyketide synthase 1 showed 44-66 identity to those of other chalcone synthase superfamily enzymes of plant origin. Further phylogenetic tree analysis revealed that Hu. serrata polyketide synthase 1 groups with other nonchalcone-produ-cing type III polyketide synthases. Indeed a recombinant enzyme expressed in Escherichia coli showed unusually versatile catalytic potential to produce various aromatic tetraketides including chalcones benzophenones phloroglucinols and acridones. In particular it is remarkable that the enzyme accepted bulky starter substrates such as 4-methoxycinnamoyl-CoA and N-methylanthraniloyl-CoA and carried out three condensations with malo-nyl-CoA to produce 4-methoxy-2 4 6 -trihydroxychalcone and 1 3-dihyd-roxy-N-methylacridone respectively. In contrast regular chalcone synthase does not accept these bulky substrates suggesting that the enzyme has a larger starter .

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