2.4.1.230	evolution	the enzyme belongs to the glycoside hydrolase family 65, GH65	-, 721869	
2.4.1.230	evolution	the enzyme is a member of glycoside hydrolase family 65, GH65	-, 720962	
2.4.1.230	evolution	the kojibiose phosphorylase belongs to the glycoside hydrolase (GH) family 65, that contains phosphorylases acting on maltose (Glc-alpha1,4-Glc), kojibiose (Glc-alpha1,2-Glc), trehalose (Glc-alpha1,alpha1,-Glc), and nigerose (Glc-alpha1,3-Glc). The loop 3 region comprising the active site of kojibiose phosphorylase is significantly longer than the active sites of other enzymes, and three residues around this loop, Trp391, Glu392, and Thr417, recognize kojibiose	736088	
2.4.1.230	additional information	structure-function relationship analysis, homology modelling, overview. Substitution of maltose phosphorylase, EC 2.4.1.8, His413-Glu421, His413-Ile418 and His413-Glu415 from loop 3, that include His413 and Glu415 presumably recognising the alpha-anomeric O-1 group of the glucose moiety at subsite 1+, by corresponding to segments from Ser426-Ala431 in trehalose phosphorylase, EC 2.4.1.64, and Thr419-Phe427 in kojibiose phosphorylase, EC 2.4.1.230, thus confers the maltose phosphorylase with phosphorolytic activity towards trehalose and kojibiose, respectively. The loop 3 in GH65 disaccharide phosphorylase is a key determinant for specificity both in phosphorolysis and in regiospecific reverse phosphorolysis	-, 720962	
2.4.1.230	additional information	structure-function relationship analysis, overview. The sequence Thr419-Phe427 is responsible for substrate specificity of the enzyme for kojibiose. The loop 3 in GH65 disaccharide phosphorylase is a key determinant for specificity both in phosphorolysis and in regiospecific reverse phosphorolysis	-, 720962	
2.4.1.230	additional information	the loop 3 region comprises the active site of kojibiose, three residues around this loop, Trp391, Glu392, and Thr417, recognize kojibiose. Trp391 and Glu392, especially the latter, are required for the kojibiose activity, active site structure and substrate binding, overview. Comparison of substrate recognition by kojibiose phosphorylase CsKP from Caldicellulosiruptor saccharolyticus and maltose phosphorylase LbMP from Lactobacillus brevis, modeling, overview	736088	
2.4.1.230	physiological function	the enzyme is involved in conversion of kojibiose into beta-D-glucose 6-phosphate, a substrate of the glycolytic pathway. Disaccharide utilization pathway via phosphorolysis in hyperthermophilic archaea	-, 725294