Disease relevance of laminaribiose

• A thioredoxin-Os4bglu12 fusion protein expressed in Escherichia coli efficiently hydrolyzed beta-(1,4)-linked oligosaccharides of 3-6 glucose residues and laminaribiose [1].

High impact information on laminaribiose

• Crystal structures of CsCBM6-3 in complex with xylotriose, cellobiose, and laminaribiose, 2.0 A, 1.35 A, and 1.0 A resolution, respectively, reveal that the binding site of CsCBM6-3 resides on the same polypeptide face as for MvX56 and AAA [2].
• Although laminaribiose gave strong inhibition of conidial binding to monocytes, cellobiose and oligosaccharides with beta 1,4-linked glucose residues were more potent as specific inhibitors of this binding over similar concentrations [3].
• The enzyme had a specificity for cellobiose, requiring Pi and Mg2+ for phosphorylation, but not for cellodextrin, gentibiose, laminaribiose, lactose, maltose, kojibiose and sucrose [4].
• The binding of banana lectin (BanLec) to laminaribiose (Glcbeta1,3Glc) and a series of novel synthetic analogues was measured by titration calorimetry to assess the contribution of the hydroxyl groups of the reducing glycosyl moiety and its 3-O-beta-substituent to binding [5].
• Phylogeny of Alariaceae, Laminariaceae, and Lessoniaceae (Phaeophyceae) based on plastid-encoded RuBisCo spacer and nuclear-encoded ITS sequence comparisons [6].

Biological context of laminaribiose

• The result of the substrate specificity for phosphorolysis was that the chimera acted on nigerose, sophorose and laminaribiose, in addition to kojibiose [7].
• In steady-state kinetic studies, an apparent decrease of laminaribiose hydrolysis was observed at high concentrations of the substrate, and the plots of glucose production versus substrate concentration were thus fitted to a modified Michaelis-Menten equation including hydrolytic and transglycosylation parameters (K(m), K(m2), k(cat), k(cat2)) [8].
• Whereas laminaribiose and diacetylchitobiose were strong inhibitors of protein binding to both glucan and chitin, lactose, maltose and sucrose were ineffective [9].

Anatomical context of laminaribiose

• This is consistent with in vitro findings that laminaribiose is a by-product of a newly identified glucosyltransferase (R. P. Hartland, G. W. Emerson & P. A. Sullivan, 1991, Proc R Soc Lond B 246, 155-160) associated with fungal cell walls [10].

Associations of laminaribiose with other chemical compounds

• Vanadium haloperoxidases from brown algae of the Laminariaceae family [11].
• HDL/BGBP has similar dissociation constants for laminaribiose (K(d)=22 mM) or heparin (K(d)=46 mM) as determined by 90 degrees light scattering [12].
• Lipoprotein aggregation resulted when HDL/BGBP interacted with phospolipid vesicles, laminaribiose (1,3-beta-glucan disaccharide) or heparin [12].

Analytical, diagnostic and therapeutic context of laminaribiose

• Size exclusion chromatography and enzymic analysis indicate that laminaribiose comprises approximately 50% of the released fraction [10].
• When laminaribiose was incubated with the enzyme, a transglycosylation product was detected by thin-layer chromatography [8].

References