The Primary Structure of the Subunit in Bacillus thermoamyloliquefaciens KP1071 Molecular Weight 540,000 Homohexameric α-Glucosidase II Belonging to the Glycosyl Hydrolase Family 31

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The gene that coded for the subunit of an molecular weight (M_r) 540,000 homohexameric α-glucosidase II (α-D-glucoside glucohydrolase, EC 3.2.1.20) produced by Bacillus thermoamyloliquefaciens KP1071 (FERM-P8477) growing at 30 to 66℃ was expressed in Escherichia coli HB101. The resulting homohexameric enzyme had a half-life of 10 min at 80℃. Its purification and characterization showed that the enzyme was identical with the native one except for the latter deleting 7 N-terminal residues found in the former. The primary sequence of the subunit with 787 residues and an M_r of 91,070 deduced from the gene was 24-34% identical to the corresponding sequences of 15 α-glucosidases in the glycosyl hydrolase family 31 from 14 eukaryotic origins and the archaeon Sulfolobus solfataricus 98/2. From the sequence analysis by the neural network mehtod of Rost and Sander [Rost, B. and Sander, C., Proteins : Struct. Funct. Genet., 19,55-72 (1994)], we inferred that α-glucosidase II might make each subunit of 3 secondary structural regions, i.e., one N-terminal β region, one central α/β region with two catalytic residues Asp407 and Asp484,and one C-terminal β region.
社団法人日本農芸化学会の論文
2000-07-23