Purification and characterization of hydroxycinnamoyl-coenzyme A: ?-hydroxypalmitic acid O-hydroxycinnamoyltransferase from tobacco (Nicotiana tabacum L.) cell-suspension cultures
Autor: | Samia Lotfy, Francine Javelle, Jonathan Negrel |
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Rok vydání: | 1996 |
Předmět: | |
Zdroj: | Planta. 199 |
ISSN: | 1432-2048 0032-0935 |
Popis: | An acyltransferase hydroxycinnamoyl-Coenzyme A: ω-hydroxypalmitic acid O-hydroxycinnamoyltransferase (HHT; EC 2.3.1.-), which transfers hydroxycinnamic acids from hydroxycinnamoyl-CoA thioesters to several hydroxylated fatty acid derivatives, was characterized from tobacco (Nicotiana tabacum L. cv. Xanthi nc) cell-suspension cultures. It exhibited the same properties as the enzyme previously detected in wound-healing potato tuber discs (Lotfy et al., 1994, Phytochemistry 35: 1419–1424), and especially a marked specificity for ω-hydroxypalmitic acid and feruloyl-CoA. It was purified 300-fold to near homogeneity from late logarithmic-phase cell suspensions. The apparent molecular mass of the native protein was 55 kDa and its isoelectric point, estimated by electrofocusing, was 4.6. The purified enzyme conjugated ferulic acid to ω-hydroxypalmitic acid and to 1-tetradecanol, its main lipidic substrates, suggesting that the same enzyme probably synthesizes the different esters of 1-alkanols and of ω-hydroxy fatty acids which are formed in vitro. |
Databáze: | OpenAIRE |
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