Zobrazeno 1 - 10 of 11 pro vyhledávání: '"Etsuo Minagawa"'
1
Cloning and nucleotide sequencing of genes encoding Mn-superoxide dismutase and class II fumarase from Thermus aquaticus YT-1
Autor: Shuichi Kaminogawa, Etsuo Minagawa, Hidemasa Motoshima, Fuji Tsukasaki
Publikováno v: Journal of Fermentation and Bioengineering. 86:21-27
A 6955-bp sequence of a Pst I- Hin dIII DNA fragment containing the manganese-superoxide dismutase (MnSOD) gene of Thermus aquaticus YT-1 was determined. The gene ( sod ) encoded a polypeptide consisting of 204 amino acid residues (the mature enzyme
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7ec038444a514bdd369c3477110b7d82
https://doi.org/10.1016/s0922-338x(98)80028-7
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2
Cloning of Genes of the Aminopeptidase T Family fromThermus thermophilusHB8 andBacillus stearothermophilusNCIB8924: Apparent Similarity to the Leucyl Aminopeptidase Family
Autor: Shuichi Kaminogawa, Hidemasa Motoshima, Etsuo Minagawa, Fuji Tsukasaki
Publikováno v: Bioscience, Biotechnology, and Biochemistry. 61:1710-1717
To obtain genes with sequence similarity to aminopeptidase T (AP-T) of Thermus aquaticus YT-1, we cloned the genes encoding aminopeptidase Th (AP-Th) from Thermus thermophilus HB8 and aminopeptidase II (APII) from Bacillus stearothermophilus NCIB8924
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be401c3fa9bdaf506bd9f449e67627e6
https://doi.org/10.1271/bbb.61.1710
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3
Purification and Characterization of a Thermostable Carboxypeptidase (CarboxypeptidaseTaq)fromThermus aquaticusYT-1
Autor: Etsuo Minagawa, Shuichi Kaminogawa, Hayao Taguchi, Hiroshi Matsuzawa, Takahisa Ohta, Sang-Hyeon Lee, Kunio Yamauchi
Publikováno v: Bioscience, Biotechnology, and Biochemistry. 56:1839-1844
A thermostable carboxypeptidase, which we named carboxypeptidase Taq, was purified from Thermus aquaticus YT-1 and characterized. The molecular weight of the enzyme was estimated to be about 56,000 and 58,000 on SDS-polyacrylamide gel electrophoresis
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::224f3a020d89ed35446ea0eacd7f758e
https://doi.org/10.1271/bbb.56.1839
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4
Molecular Cloning and Nucleotide Sequence of the Aminopeptidase T Gene ofThermus aquaticusYT-1 and Its High-level Expression inEscherichia coli
Autor: Etsuo Minagawa, Norihiro Azuma, Hiroshi Matsuzawa, Shuichi Kaminogawa, Takahisa Ohta, Kunio Yamauchi, Hidemasa Motoshima, Makoto Ono
Publikováno v: Agricultural and Biological Chemistry. 54:2385-2392
Aminopeptidase T (AP-T) is a metallo-dependent dimeric enzyme of Thermus aquaticus YT-1, an extremely thermophilic bacterium. We cloned the AP-T gene from T. aquaticus YT-1 into Escherichia coli using a synthetic oligonucleotide as a hybridization pr
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4d1e0ae5ae6095d4388f6ae93fe95693
https://doi.org/10.1080/00021369.1990.10870335
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6
The active site of carboxypeptidase Taq possesses the active-site motif His-Glu-X-X-His of zinc-dependent endopeptidases and aminopeptidases
Autor: Hayao Taguchi, Takahisa Ohta, Etsuro Yoshimura, Sang-Hyeon Lee, Shuichi Kaminogawa, Etsuo Minagawa, Hiroshi Matsuzawa
Publikováno v: Protein engineering. 9(6)
Carboxypeptidase (CPase) Taq possesses the His-Glu-X-X-His sequence, which is the consensus sequence in the active site of zinc-dependent endopeptidases and amino-peptidases, at positions 276-280. Amino acid replacement of the conserved His and Glu d
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b95ae47eb5a105c74b447787eed7b81e
https://pubmed.ncbi.nlm.nih.gov/8862545
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7
Carboxypeptidase Taq, a thermostable zinc enzyme, from Thermus aquaticus YT-1: molecular cloning, sequencing, and expression of the encoding gene in Escherichia coli
Autor: Hayao Taguchi, Hiroshi Matsuzawa, Shuichi Kaminogawa, Takahisa Ohta, Sang-Hyeon Lee, Etsuo Minagawa, Etsuro Yoshimura
Publikováno v: Bioscience, biotechnology, and biochemistry. 58(8)
The gene for carboxypeptidase Taq, a thermostable metallo-carboxypeptidase from Thermus aquaticus YT-1, was cloned and sequenced. The gene comprised an open reading frame of 1,536 base pairs with a GTG initiation codon and a TGA termination codon, wh
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de22497e406f5355e3e08c45523f3961
https://pubmed.ncbi.nlm.nih.gov/7765282
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8
Isolation and characterization of a thermostable aminopeptidase(aminopeptidase T) from Thermus aquaticus YT-1, an extremely thermophilic bacterium
Autor: Etsuo Minagawa, Shuichi Kaminogawa, Hiroshi Matsuzawa, Takahisa Ohta, Kunio Yamauchi
Publikováno v: Agricultural and Biological Chemistry. 52:1755-1763
A thermostable aminopeptidase, called aminopeptidase T, from the extract of Thermus aquaticus YT-1 was purified and characterized. The enzyme had a dimeric structure, its relative molecular mass being 108, 000 by gel filtration, and 48, 000 by SDS-PA
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c543e75787283b397ce907608cccbedd
https://doi.org/10.1271/bbb1961.52.1755
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9
Exopeptidase profiles of bifidobacteria
Autor: Hidemasa Motoshima, Etsuo Minagawa, Shuichi Kaminogawa, Kunio Yamauchi, Fuji Tsukasaki
Publikováno v: Journal of Nutritional Science and Vitaminology. 31:599-606
The exopeptidase activities of five different strains of bifidobacteria occurring habitually in healthy human intestinal canal were measured on 61 synthetic substrates. The cluster analysis, based on the results, indicates that four strains, with the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0dc5f7ae6c5714dcadfe64b9e8037f7e
https://doi.org/10.3177/jnsv.31.599
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