| the primary structure of the subunit in bacillus thermoamyloliquefaciens kp1071 molecular weight 540,000 homohexameric alpha-glucosidase ii belonging to the glycosyl hydrolase family 31. | the gene that coded for the subunit of an molecular weight (mr) 540,000 homohexameric alpha-glucosidase ii (alpha-d-glucoside glucohydrolase, ec 3.2.1.20) produced by bacillus thermoamyloliquefaciens kp1071 (ferm-p8477) growing at 30 to 66 degrees c was expressed in escherichia coli hb101. the resulting homohexameric enzyme had a half-life of 10 min at 80 degrees c. its purification and characterization showed that the enzyme was identical with the native one except for the latter deleting 7 n-t ... | 2000 | 10945254 |
| biochemical properties and substrate recognition mechanism of gh31 α-glucosidase from bacillus sp. ahu 2001 with broad substrate specificity. | α-glucosidases are ubiquitous enzymes that hydrolyze the α-glucosidic linkage at the non-reducing end of substrates. in this study, we characterized an α-glucosidase (bspag31a) belonging to glycoside hydrolase family 31 from bacillus sp. ahu 2001. recombinant bspag31a, produced in escherichia coli, had high hydrolytic activity toward maltooligosaccharides, kojibiose, nigerose, and neotrehalose. this is the first report of an α-glucosidase with high activity toward neotrehalose. the transglucosyl ... | 2015 | 25450253 |
| bacillus thermoamyloliquefaciens kp1071 alpha-glucosidase ii is a thermostable m(r) 540,000 homohexameric alpha-glucosidase with both exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities. | alpha-glucosidase ii of the facultative thermophile bacillus thermoamyloliquefaciens kp1071 (ferm-p8477; growth over 30-66 degrees c) was purified to a homogeneous state. its m(r) was estimated as 90000 by sds/page. however, the enzyme behaved as an active mr 540000 protein on gel filtration with each of two gels of different matrices as well as on gel electrophoresis under native conditions. the enzyme was not glycosylated. its isoelectric point was estimated as 5.7. the n-terminal sequence of ... | 1997 | 9128733 |
| assignment of bacillus thermoamyloliquefaciens kp1071 alpha-glucosidase i to an exo-alpha-1,4-glucosidase, and its striking similarity to bacillary oligo-1,6-glucosidases in n-terminal sequence and in structural parameters calculated from the amino acid composition. | alpha-glucosidase i of bacillus thermoamyloliquefaciens kp1071 (ferm p8477, facultative thermophile) was purified to homogeneity. the relative molecular mass was estimated to be 62,000 da. from its catalytic properties, the enzyme has been assigned to an exo-alpha-1,4-glucosidase. the enzyme shares its antigenic groups in part with bacillus stearothermophilus atcc12016 (obligate thermophile) exo-alpha-1,4-glucosidase. these exo-alpha-1,4-glucosidases strikingly resemble oligo-1,6-glucosidases fr ... | 1992 | 1555585 |