99877-83-5Relevant articles and documents
Gallotannin biosynthesis: Purification of β-glucogallin: 1,2,3,4,6-pentagalloyl-β-d-glucose galloyltransferase from sumac leaves in honour of professor G. H. Neil towers 75th birthday
Niemetz, Ruth,Gross, Georg G.
, p. 327 - 332 (2007/10/03)
An enzyme from leaves of staghorn sumac (Rhus typhina) that catalysed the galloylation of 1,2,3,4,6penta-O-galloyl-β-D-glucose to the gallotannin, 3-O-digalloyl-l,2,4,6-tetra-0-galloyl-β-D-glucose, was purified more than 500-fold to apparent homogeneity. β-Glucogallin (l-0-galloyl-β-D-glucopyranose) served as activated acyl donor in this conversion. For the native enzyme, a M, value of 170,000 was determined by gel filtration, while a single polypeptide band of Mr 42,000 was detected by SDS-PAGE. The acyltransferase had pH and temperature optima of 4-4.5 and 25°, respectively, and was most stable between pH 3 and 4.5. Besides the major substrate, pentagalloylglucose, also 1,2,3,6-tetragalloylglucose and hexa- to nona-substituted gallotannins were accepted as minor substrates by this new enzyme for which the systematic name β-glucogallin: l,2,3,4,6-pentagalloyl-β-D-glucose (3-O-galloyl)-galloyltransferase" (EC 2.3.1.-) is proposed.
