Chalcone synthase homologues from Humulus lupulus: some enzymatic properties and expression
2006
Novak, P.(Akademie Ved, Ceske Budejovice (Czech Republic). Ustav Molekularni Biologie Rostlin) | Krofta, K.(Chmelarsky Inst., Zatec (Czech Republic)) | Matousek, J.(Akademie Ved, Ceske Budejovice (Czech Republic). Ustav Molekularni Biologie Rostlin) E-mail:[email protected]
Enzymatic properties of four chalcone synthase homologues, CHS_H1, VPS, CHS 2 and CHS 4, from Humulus lupulus were investigated after heterologous expression in Escherichia coli. Both VPS and CHS_H1 can utilize isovaleryl-CoA and isobutyryl-CoA as substrates producing compounds with positions in thin layer chromatography characteristic for phloroisovalerophenone and phloroisobutyrophenone. The formation of naringenin chalcone can be catalyzed primarily by CHS_H1. The ability of VPS to perform chalcone synthase reaction is very limited. Since only CHS_H1 has true chalcone synthase activity, this enzyme can be considered a key enzyme in prenylflavonoid biosynthesis. Both CHS 2 and CHS 4 utilized isovaleryl-CoA and isobutyryl-CoA as substrates, but the reactions were prematurely terminated. High expression of chalcone synthase-like genes were found in maturating hop cones of cultivars with high bitter acid content (Agnus, Magnum, Target).
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