Abstract
Hydroxycinnamoyltransferases (HCTs) catalyze the transfer of the cinnamoyl moiety from hydroxycinnamoyl-CoA to various acceptors such as shikimic acid, quinic acid, hydroxylated acid, and glycerol. Four rice HCT homologues (OsHCT1–4) to tobacco HST were cloned, and OsHCT4 was expressed in Escherichia coli as a glutathione S-transferase fusion protein. Using the purified recombinant protein and biotransformation techniques, whether OsHCT4 shows hydroxycinnamoyltransferase activity with a variety of acyl group acceptors was investigated. The results of high performance liquid chromatography (HPLC) and mass spectrometry (MS) established that OsHCT4 mediated the trans-esterification of glycerol as well as shikimic acid in the presence of hydroxycinnamoyl-CoA. The structure of the reaction product was determined using nuclear magnetic resonance spectroscopy (NMR). E. coli cells co-expressing 4CL (4-coumarate:coenzyme A ligase) and OsHCT4 converted p-coumaric acid, ferulic acid, and caffeic acid into the corresponding glycerides. While this conversion is very efficient in vitro, the physiological significant in rice is currently unknown.
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