High impact information on Sophorose

• Cellulase induction by sophorose was not affected by ace2 deletion [1].
• Electrophoretic mobility shift assays, using cell-free extracts, identified induction-specific protein-DNA complexes: one complex of high mobility was observed under basal, noninduced conditions (glucose) with xyn2, which was in part replaced by a slow-migrating complex upon induction by xylan or sophorose [2].
• Deletion of ace1 resulted in an increase in the expression of all the main cellulase genes and two xylanase genes in sophorose- and cellulose-induced cultures, indicating that ACEI acts as a repressor of cellulase and xylanase expression [3].
• Addition of 2 mM sophorose, a putative inducer of cellulase gene expression, to such cultures induced the transcription of egl1 and egl2 and restored the ability to grow on cellulose [4].
• Optimal activity with PNPG and cellobiose as the substrates is at pH 6.2 and 50 degrees C. The enzyme has high activity against sophorose (beta-1,2-glucobiose) and laminaribiose (beta-1,3-glucobiose) but has no activity against gentiobiose (beta-1,6-glucobiose) [5].

Biological context of Sophorose

• Repression of beta-glucosidase reduces sophorose hydrolysis and thus may increase cellulase induction [6].
• The induction response to sophorose concentration, although complicated by the metabolism of sophorose, shows saturation kinetics [7].
• The involvement of cytochrome P450 in the synthesis of sophorose lipid by the hydroxylation of long-chain fatty acids was suggested from a simultaneous increase of cellular P450 content [8].
• Sophorose induction of the promoter was retained even in deletion derivatives lacking sequences upstream of position -161, which retained about 70 bp upstream of the transcription start point and only 30 bp upstream of the TATA box [9].
• The result of the substrate specificity for phosphorolysis was that the chimera acted on nigerose, sophorose and laminaribiose, in addition to kojibiose [10].

Anatomical context of Sophorose

• Cellooligosaccharides and sophorose induced endoglucanase synthesis in mycelia, conidia and protoplasts [11].

Associations of Sophorose with other chemical compounds

• The cellulase inducer sophorose was rapidly catabolized to CO2 and H2O by Trichoderma: only small amounts were used to induce the synthesis of cellulase [12].
• The disaccharide sophorose induces Trichoderma to increase a soluble intracellular b-glucosidase that hydrolyses cellobiose, sophorose, and p-nitrophenyl-b-D-glucopyranoside [13].
• A beta-glucosidase from sweet almonds degraded sophorose but not the intact glucan [14].
• In addition to the hydrolysis of p-nitrophenyl-beta-glucoside, the enzyme was also active against several other aryl-beta-glucosides as well as a range of beta-linked oligoglucosides including laminaribiose, gentiobiose, cellobiose, and sophorose [15].
• L-Sorbose has previously been assumed to stimulate cellulase formation in an indirect manner, different from that of sophorose in Trichoderma reesei [16].

Gene context of Sophorose

• The mechanism of this regulation was studied by examining pdi1 mRNA levels under conditions where the extracellular enzymes are induced by sophorose, as well as in the strain RutC-30, which is mutant for the glucose repressor gene cre1 [17].
• Endo-A transferred high-mannose-type oligosaccharides more efficiently to beta-linked disaccharides (cellobiose, gentiobiose, sophorose, and laminaribiose) than to alpha-linked disaccharides (isomaltose, maltose, nigerose, kojibiose, and trehalose) as acceptor substrates [18].

Analytical, diagnostic and therapeutic context of Sophorose

• The differential regulation of expression of those 20 genes by sophorose in wild-type and mutant was verified by Northern blotting [19].

References