Rice family GH1 glycoside hydrolases with β-d-glucosidase and β-d-mannosidase activities Export

@article{citeulike:5827304, abstract = {Plant β- d -mannosidases and a rice β- d -glucosidase, Os3BGlu7, with weak β- d -mannosidase activity, cluster together in phylogenetic analysis. To investigate the relationship between substrate specificity and amino acid sequence similarity in family GH1 glycoside hydrolases, Os3BGlu8 and Os7BGlu26, putative rice β- d -glucosidases from this cluster, and a β- d -mannosidase from barley (rHvBII), were expressed in Escherichia coli and characterized. Os3BGlu8, the amino acid sequence and molecular model of which are most similar to Os3BGlu7, hydrolysed 4-nitrophenyl-β- d -glucopyranoside (4NPGlc) faster than 4-nitrophenyl-β- d -mannopyranoside (4NPMan), while Os7BGlu26, which is most similar to rHvBII by these criteria, hydrolysed 4NPMan faster than 4NPGlc. All the enzymes hydrolyzed cellooligosaccharides with increased hydrolytic rates as the degree of polymerization increased from 3–6, but only rHvBII hydrolyzed cellobiose with a higher k cat / K m value than cellotriose. This was primarily due to strong binding of glucosyl residues at the + 2 subsite for the rice enzymes, and unfavorable interactions at this subsite with rHvBII.}, author = {Kuntothom, Teerachai and Luang, Sukanya and Harvey, Andrew J. and Fincher, Geoffrey B. and Opassiri, Rodjana and Hrmova, Maria and Ketudat Cairns, James R.}, citeulike-article-id = {5827304}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.abb.2009.09.004}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0003986109002926}, day = {18}, doi = {10.1016/j.abb.2009.09.004}, issn = {00039861}, journal = {Archives of Biochemistry and Biophysics}, keywords = {family}, month = {November}, number = {1-2}, pages = {85--95}, posted-at = {2009-10-31 17:06:42}, priority = {2}, title = {Rice family GH1 glycoside hydrolases with β-d-glucosidase and β-d-mannosidase activities}, url = {http://dx.doi.org/10.1016/j.abb.2009.09.004}, volume = {491}, year = {2009} }

TY - JOUR ID - citeulike:5827304 L3 - citeulike-article-id:5827304 N2 - Plant β- d -mannosidases and a rice β- d -glucosidase, Os3BGlu7, with weak β- d -mannosidase activity, cluster together in phylogenetic analysis. To investigate the relationship between substrate specificity and amino acid sequence similarity in family GH1 glycoside hydrolases, Os3BGlu8 and Os7BGlu26, putative rice β- d -glucosidases from this cluster, and a β- d -mannosidase from barley (rHvBII), were expressed in Escherichia coli and characterized. Os3BGlu8, the amino acid sequence and molecular model of which are most similar to Os3BGlu7, hydrolysed 4-nitrophenyl-β- d -glucopyranoside (4NPGlc) faster than 4-nitrophenyl-β- d -mannopyranoside (4NPMan), while Os7BGlu26, which is most similar to rHvBII by these criteria, hydrolysed 4NPMan faster than 4NPGlc. All the enzymes hydrolyzed cellooligosaccharides with increased hydrolytic rates as the degree of polymerization increased from 3–6, but only rHvBII hydrolyzed cellobiose with a higher k cat / K m value than cellotriose. This was primarily due to strong binding of glucosyl residues at the + 2 subsite for the rice enzymes, and unfavorable interactions at this subsite with rHvBII. IS - 1-2 JF - Archives of Biochemistry and Biophysics SN - 00039861 EP - 95 TI - Rice family GH1 glycoside hydrolases with β-d-glucosidase and β-d-mannosidase activities VL - 491 SP - 85 KW - family AU - Kuntothom, Teerachai AU - Luang, Sukanya AU - Harvey, Andrew AU - Fincher, Geoffrey AU - Opassiri, Rodjana AU - Hrmova, Maria AU - Ketudat Cairns, James PY - 2009/11/18/ UR - http://dx.doi.org/10.1016/j.abb.2009.09.004 ER -