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

• Published in: Biochemical journal Vol. 252; no. 1; pp. 199 - 206
• Main Authors: Andrews, D.L, Beames, B, Summers, M.D, Park, W.D
• Format: Journal Article
• Language: English
• Published: England 15-05-1988
• Subjects: Acyltransferases - metabolism; Autographa californica; Carboxylic Ester Hydrolases; Chromatography, Thin Layer; cloning; Cloning, Molecular; DNA Viruses; DNA, Recombinant; enzyme activity; Genetic Vectors; glycoproteins; hydrolases; Immunoelectrophoresis; Insect Viruses - genetics; Lipid Metabolism; patatin; plant proteins; Plant Proteins - genetics; Plant Proteins - isolation & purification; Plant Proteins - metabolism; polyhedrosis viruses; Solanum tuberosum; Solanum tuberosum - enzymology; Solanum tuberosum - metabolism; Structure-Activity Relationship; Substrate Specificity; vectors
• ISSN: 0264-6021; 1470-8728
• DOI: 10.1042/bj2520199

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.