Characterization of the lipid acyl hydrolase activity of the major potato (Solanum tuberosum) tuber protein, patatin, by cloning and abundant expression in a baculovirus vector. Academic Article uri icon

abstract

  • Patatin is a family of glycoproteins that accounts for 30-40% of the total soluble protein in potato (Solanum tuberosum) tubers. This protein has been reported not only to serve as a storage protein, but also to exhibit enzymic activity. By using a baculovirus system to express protein from the patatin cDNA clone pGM01, it was unambiguously shown that the patatin coded by this DNA has lipid acyl hydrolase and acyltransferase activities. The enzyme is active with phospholipids, monoacylglycerols and p-nitrophenyl esters, moderately active with galactolipids, but is apparently inactive with di- and tri-acylglycerols.

published proceedings

  • Biochem J

altmetric score

  • 6

author list (cited authors)

  • Andrews, D. L., Beames, B., Summers, M. D., & Park, W. D.

citation count

  • 210

complete list of authors

  • Andrews, DL||Beames, B||Summers, MD||Park, WD

publication date

  • May 1988