Disease relevance of Kojibiose

• The glucosyl transfer reaction of kojibiose phosphorylase (KPase) from Thermoanaerobacter brockii ATCC35047 was examined using cyclo-{-->6)-alpha-d-Glcp-(1-->3)-alpha-d-Glcp-(1-->6)-alpha-d-Glcp-(1-->3)-alpha-d-Glcp-(1-->} (CTS) as an acceptor [1].
• Kojibiose phosphorylase was efficiently overexpressed in Escherichia coli JM109 [2].

High impact information on Kojibiose

• Kojibiose was found to inhibit glucosidase action not only on the free oligosaccharide but also on protein-bound one [3].
• Construction and characterization of chimeric enzymes of kojibiose phosphorylase and trehalose phosphorylase from Thermoanaerobacter brockii [4].
• The result of the substrate specificity for phosphorolysis was that the chimera acted on nigerose, sophorose and laminaribiose, in addition to kojibiose [4].
• For disaccharides, the rate of hydrolysis decreased in the following order: maltose divided by nigerose greater than kojibiose greater than isomaltose [5].
• While the combining site of 870 protein appears to bind alpha-D-mannopyranosyl, alpha-D-galactopyranosyl and alpha-D-glucopyranosyl residues, the combining site of 384 protein can accommodate both the alpha (1----2)-linked glucobiose (kojibiose) and alpha-D-galactopyranosyl but not the alpha-D-mannopyranosyl structure [6].

Chemical compound and disease context of Kojibiose

• Acceptor recognition of kojibiose phosphorylase from Thermoanaerobacter brockii: syntheses of glycosyl glycerol and myo-inositol [7].

Biological context of Kojibiose

• Each of three amino acid substitutions, D362N, K614Q and E642Q, caused a complete loss of kojibiose phosphorylase activity [2].
• Enhancement of thermostability of kojibiose phosphorylase from Thermoanaerobacter brockii ATCC35047 by random mutagenesis [8].

Analytical, diagnostic and therapeutic context of Kojibiose

• Random mutation by error-prone PCR was introduced into kojibiose phosphorylase from Thermoanaerobacter brockii ATCC35047 [8].

References