Mutational and crystallographic analyses of Thermoplasma acidophilum D-aldohexose dehydrogenase C-teminal deletion mutants
نویسندگان
چکیده
Taiki NISHIOKA, Yoshiaki YASUTAKE, Yoshiaki NISHIYA, Noriko TAMURA, and Tomohiro TAMURA Graduate School of Agriculture, Hokkaido University, N9W9, Kita-ku, Sapporo 060-8589, Japan Bioproduction research institute, National Institute of Advanced Industrial Science and Technology (AIST), 2-17-2-1 Tsukisamu-Higashi, Toyohira-ku, Sapporo 062-8517, Japan Tsuruga Institute of Biotechnology, Toyobo Co., Ltd., 10-24, Toyo-cho, Tsuruga 914-0047, Japan
منابع مشابه
Analysis of bacterial glucose dehydrogenase homologs from thermoacidophilic archaeon Thermoplasma acidophilum: finding and characterization of aldohexose dehydrogenase.
The NADP(+)-preferring glucose dehydrogenase from thermoacidophilic archaeon Thermoplasma acidophilum has been characterized, and its crystal structure has been determined (Structure, 2:385-393, 1994). Its sequence and structure are not homologous to bacterial NAD(P)(+)-dependent glucose dehydrogenases, and its molecular weight is also quite defferent. On the other hand, three functionally unkn...
متن کاملStructural insights into unique substrate selectivity of Thermoplasma acidophilum D-aldohexose dehydrogenase.
The D-aldohexose dehydrogenase from the thermoacidophilic archaea Thermoplasma acidophilum (AldT) belongs to the short-chain dehydrogenase/reductase (SDR) superfamily and catalyzes the oxidation of several monosaccharides with a preference for NAD(+) rather than NADP(+) as a cofactor. It has been found that AldT is a unique enzyme that exhibits the highest dehydrogenase activity against D-manno...
متن کاملStructural and mutational analysis of tRNA intron-splicing endonuclease from Thermoplasma acidophilum DSM 1728: catalytic mechanism of tRNA intron-splicing endonucleases.
In archaea, RNA endonucleases that act specifically on RNA with bulge-helix-bulge motifs play the main role in the recognition and excision of introns, while the eukaryal enzymes use a measuring mechanism to determine the positions of the universally positioned splice sites relative to the conserved domain of pre-tRNA. Two crystallographic structures of tRNA intron-splicing endonuclease from Th...
متن کاملStructural and Mutational Analysis of tRNA-Intron Splicing Endonuclease from Thermoplasma acidophilum DSM 1728: The Catalytic Mechanism of tRNA-Intron Splicing Endonucleases
In archaea, RNA endonucleases which act specifically on RNA having bulge-helix-bulge (BHB) motifs play the main role in the recognition and excision of introns while the eukaryal enzymes use a measuring mechanism to determine the position of the universally positioned splice sites relative to the conserved domain of pre-tRNA. Two crystallographic structures of tRNA-intron splicing endonuclease ...
متن کاملPurification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum.
Glucose dehydrogenase was purified to homogeneity from the thermoacidophilic archaebacterium Thermoplasma acidophilum. The enzyme is a tetramer of polypeptide chain Mr 38,000 +/- 3000, it is catalytically active with both NAD+ and NADP+ cofactors, and it is thermostable and remarkably resistant to a variety of organic solvents. The amino acid composition was determined and compared with those o...
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