S Asano
Kyoto University
5 Papers
147 Citations
S Asano is an academic researcher from Kyoto University. The author has contributed to research in topics: Amino acid & Peptide sequence. The author has an hindex of 4, co-authored 5 publications.
Chat about Author
Papers
The primary structure of thermostable D-amino acid aminotransferase from a thermophilic Bacillus species and its correlation with L-amino acid aminotransferases.
Katsuyuki Tanizawa,S Asano,Yasuo Masu,Seiki Kuramitsu,Hiroyuki Kagamiyama,H. Tanaka,Kenji Soda +6 more
TL;DR: The sequence homology suggests that the structural genes for D-amino acid and L-branched chain amino acid aminotransferases evolved from a common ancestral gene.
114
Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species. Purification, characterization, and active site sequence determination.
TL;DR: D-Amino acid aminotransferase was found in several thermophilic Bacillus species and purified to homogeneity from the best producer, Bacillus sp.
93
Preliminary X-ray data for a d-amino acid amino-transferase from a novel thermophilic Bacillus
Barry L. Stoddard,Lynne Howell,S Asano,Kenji Soda,Katsuyuki Tanizawa,Dagmar Ringe,Gregory A. Petsko +6 more
TL;DR: Crystals of the D-amino acid aminotransferase (D-ATA) from a novel thermophilic Bacillus species (Escherichia coli pICT113 cloned gene product) have been examined by X-ray analysis.
18
Thermostable alanine racemase of Bacillus stearothermophilus. Construction and expression of active fragmentary enzyme.
Hirohide Toyama,Katsuyuki Tanizawa,Tohru Yoshimura,S Asano,Young Hee Lim,Nobuyoshi Esaki,Kenji Soda +6 more
TL;DR: A mutant gene is constructed that tandemly encodes the two polypeptides of the Bacillus stearothermophilus enzyme subunit that cleaved at the position corresponding to the predicted hinge region and was immunologically identical to the wild-type enzyme.
15
D-Amino Acid Aminotransferase from a Thermophile, Bacillus SP. YM-1: Enzymological Properties, Cloning of the Gene, and the Amino Acid Sequence
Katsuyuki Tanizawa,Yasuo Masu,S Asano,Hidehiko Tanaka,Kenji Soda +4 more
- 01 Jan 1987
TL;DR: A thermophile which grows in a medium containing D-amino acids as a nitrogen source from soil and identified as a new Bacillus species showed a very high activity of D-Amino acid aminotransferase, which shows high sequence homology with that of branched-chain amino acid am inotransFERase of E. coli.
6