Glucose Polyester Biosynthesis. Purification and Characterization of a Glucose Acyltransferase
- 1 October 1999
- journal article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 121 (2) , 453-460
- https://doi.org/10.1104/pp.121.2.453
Abstract
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.Keywords
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