The primary structure of thermostable D-amino acid aminotransferase from a thermophilic Bacillus species and its correlation with L-amino acid aminotransferases.

Tanizawa, K; Asano, S; Masu, Y; Kuramitsu, S; Kagamiyama, H; Tanaka, H; Soda, K

Tanizawa, K; Asano, S; Masu, Y; Kuramitsu, S; Kagamiyama, H; Tanaka, H; Soda, K.

Affiliation

Tanizawa K; Institute for Chemical Research, Kyoto University, Japan.

J Biol Chem ; 264(5): 2450-4, 1989 Feb 15.

Article in En | MEDLINE | ID: mdl-2644261

Subject(s)

Bacillus/enzymology; Transaminases/genetics; Amino Acid Sequence; Bacillus/genetics; Base Sequence; Cloning, Molecular; D-Alanine Transaminase; Escherichia coli/genetics; Genes; Genes, Bacterial; Molecular Sequence Data; Plasmids; Protein Conformation; Restriction Mapping; Sequence Homology, Nucleic Acid

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Collection: 01-internacional Database: MEDLINE Main subject: Bacillus / Transaminases Language: En Journal: J Biol Chem Year: 1989 Type: Article Affiliation country: Japan

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