H. Tanaka
Kyoto University
25 Papers
325 Citations
H. Tanaka is an academic researcher from Kyoto University. The author has contributed to research in topics: Amino acid & Pyridoxal. The author has an hindex of 10, co-authored 25 publications.
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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.
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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.
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Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization.
Moon-Hee Sung,Katsuyuki Tanizawa,H. Tanaka,Seiki Kuramitsu,Hiroyuki Kagamiyama,K. Hirotsu,A. Okamoto,T. Higuchi,Kenji Soda +8 more
TL;DR: The gene encoding aspartate aminotransferase of a thermophilic Bacillus species, YM-2, has been cloned and expressed efficiently in Escherichia coli and the primary structure of the enzyme was deduced from nucleotide sequences of the gene and confirmed mostly by amino acid sequences of tryptic peptides.
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Purification and characterization of thermostable aspartate aminotransferase from a thermophilic Bacillus species.
TL;DR: Aspartate aminotransferase (EC 2.1) was purified to homogeneity from cell extracts of a newly isolated thermophilic bacterium, Bacillus sp.
54
Purification and characterization of selenocysteine beta-lyase from Citrobacter freundii.
TL;DR: The purification and characterization of bacterial selenocysteine beta-lyase, an enzyme which specifically catalyzes the cleavage of L-selenocysteines to L-alanine and Se0, are presented and the catalytic properties are very similar.
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