the enzyme prefers alpha-L arabinofuranosidase-treated arabinogalactan-proteins from radish roots (151% activity) and radish leaves (87% activity) compared to native ones from radish roots (36% activity) and leaves (28% activity)
galactan from Prototheca zopfii, which has a high proportion of beta-1,6-linked galactosyl residues, the extent of hydrolysis of the carbohydrate portion of a radish root arabinogalactan-protein AGP increases when alpha-L-arabinofuranosyl residues attached to beta-1,6-linked galactosyl side chains of the AGP are removed in advance, the enzyme releases galactose, beta-1,6-galactobiose, and 4-O-methyl-beta-glucuronosyl-1,6-galactose as major hydrolysis products when allowed to act exhaustively on the modified AGP, overview
plant type II arabinogalactans consisting of beta-(1,3)- and beta-(1,6)-galactan side chains connected to each other by (1,3)(1,6)-linked branch points. The O-3 and O-6 positions are substituted with terminal arabinosyl residues
the enzyme fails to act on gum arabic, beta-(1->6)-galactobiose beza-(1->4)-galactan from lupin, beta-(1->3)(1->4)-glucan from barley, beta-(1->3)(1->6)-glucan from Laminaria digitata, beta-(1->6)-glucan from Umbilicaria papullosa, carboxymethyl-curdlan (beta-(1->3)-glucan), carboxymethyl-cellulose (beta-(1->4)-glucan), galactomannan from guar, galactomannan from locust bean, beta-(1->4)-xylan from birchwood, arabino-beta-(1->4)-xylan from wheat flour, arabinan (alpha-(1->3)(1->5)-arabinan), and debranched arabinan (alpha-(1->5)-arabinan)
substrate preparations and specificity, the endo-galactanase hydrolyzes specifically beta-1,6-galactooligosaccharides with a degree of polymerization higher than 3 and their acidic derivatives with 4-O-methyl-glucosyluronic or glucosyluronic groups at the nonreducing terminals, oveview
growth of both races with glucose show basal transcription levels of enzyme. When glucose is replaced with arabinogalactan, xylan or plant cell walls, gene ebg transcription markedly increases in pathogenic race 1472 but not in non-pathogenic race 0
endo-breta-(1,6)-D-galactanase is a debranching hemicellulase that catalyzes the hydrolysis of beta-(1,6)-galactosyl side chains in arabinogalactans (AGs), producing beta-(1,6)-galacto-oligomers and beta-(1,6)-D-galactobiose. The enzyme plays a critical role in cell wall degradation. Arabinogalactan proteins (AGPs) are putative co-receptors in signaling pathways that function during growth and plant developmen. AGPs also play a key role in both beneficial and pathogenic root-microorganism interactions. They are essential for root cells to recognize beneficial microorganisms as well for root cells to trigger localized and efficient defense responses to control pathogenic organisms. Since the carbohydrate groups in AGPs are critical for their function, it is conceivable to hypothesize that the pathogenic race of Colletotrichum lindemuthianum, which more rapidly expresses gene ebg at higher levels in the presence of plant cell wall polysaccharides, is better adapted to degrade AGPs for the establishment of the infection as the non-pathogenic race
putative DNA-binding sites for Cre, Xlnr, ACEI, PacC and Gal4 transcriptional factors are predicted in ebg genes from Colletotrichum species. Identification of potential functional and structural domains, protein structure homology modelling and structure comaprisons. In enzyme EBG, the catalytic proton donor E191 is positioned in a coil and the catalytic nucleophile E293 is positioned in a beta-strand
recombinant maltose-binding-protein fusion enzyme from Escherichia coli strain DH5alpha, by cation exchange and amylose affinity chromatography, followed by hydrophobic interaction chromatography, native enzyme 88fold from strain S12 culture filtrate by anion exchange and hydrophobic interaction chromatography, followed by cation exchange chromatography, dialysis and gel filtration
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growth of both races with glucose show basal transcription levels of ebg. When glucose is replaced with arabinogalactan, xylan or plant cell walls, gene ebg transcription markedly increased in pathogenic race 1472 but not in non-pathogenic race 0
Villa-Rivera, M.; Zavala-Paramo, M.; Conejo-Saucedo, U.; Lopez-Romero, E.; Lara-Marquez, A.; Cano-Camacho, H.
Differences in the expression profile of endo-beta-(1,6)-D-galactanase in pathogenic and non-pathogenic races of Colletotrichum lindemuthianum grown in the presence of arabinogalactan, xylan or Phaseolus vulgaris cell walls