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
Rok vydání:	1996
Předmět:	chemistry.chemical_classification biology Isoelectric focusing Nicotiana tabacum Coenzyme A Plant Science biology.organism_classification Ferulic acid chemistry.chemical_compound Isoelectric point Enzyme Biochemistry chemistry Acyltransferase Genetics Nicotiana
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
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::14e9a98de5569781c95c5f1aeb2558c7 https://doi.org/10.1007/bf00195742 Zobrazit plný text záznamu Full text from SpringerLink