Glucose Polyester Biosynthesis. Purification and Characterization of a Glucose Acyltransferase
| Autor: | Alice X. Li, Nancy T. Eannetta, John C. Steffens, Gurdev S. Ghangas |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Physiology
Molecular Sequence Data macromolecular substances Plant Science Acetates Biology Chromatography Affinity Acylation chemistry.chemical_compound Solanum lycopersicum Affinity chromatography Biosynthesis Genetics Amino Acid Sequence Molecular mass Chromatofocusing Chromatography Ion Exchange Heterotetramer Peptide Fragments carbohydrates (lipids) Kinetics Glucose Isoelectric point Biochemistry chemistry Acyltransferase Electrophoresis Polyacrylamide Gel Indicators and Reagents lipids (amino acids peptides and proteins) Acyltransferases Research Article |
| Zdroj: | Plant Physiology. 121:453-460 |
| ISSN: | 1532-2548 0032-0889 |
| DOI: | 10.1104/pp.121.2.453 |
| Popis: | Glandular trichomes of the wild tomato species Lycopersicon pennellii secrete 2,3,4-O-tri-acyl-glucose (-Glc), which contributes to insect resistance. A Glc acyltransferase catalyzes the formation of diacyl-Glc by disproportionating two equivalents of 1-O-acyl-β-Glc, a high-energy molecule formed by a UDP-Glc dependent reaction. The acyltransferase was purified 4,900-fold from L. pennellii leaves by polyethylene glycol fractionation, diethylaminoethyl chromatography, concanavalin A affinity chromatography, and chromatofocusing. The acyltransferase possesses an isoelectric point of 4.8, a relative molecular mass around 110 kD, and is composed of 34- and 24-kD polypeptides as a heterotetramer. The 34- and 24-kD proteins were partially sequenced. The purified enzyme catalyzes both the disproportionation of 1-O-acyl-β-Glcs to generate 1,2-di-O-acyl-β-Glc and anomeric acyl exchange between 1-O-acyl-β-Glc and Glc. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|