Výsledky vyhledávání - "Issei Yoshioka"

Stabilization ofFlavobacterium meningosepticumGlycerol Kinase by Introduction of a Hydrogen Bond

Autor: Toshihisa Ohshima, Hideki Takehara, Haruhiko Sakuraba, Hideo Misaki, Issei Yoshioka, Shin-ichi Sakasegawa

Publikováno v: Bioscience, Biotechnology, and Biochemistry. 66:1374-1377

The thermostability of Flavobacterium meningosepticum glycerol kinase was increased by the change from Ser329 to Asp [Protein Eng., 14, 663-667 (2001)]. Based on a three-dimensional structure model of the mutant, we have postulated that a new charged

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::447a5987269ba716ddf32dd84fc1f5ad
https://doi.org/10.1271/bbb.66.1374

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Stable Ammonia-specific NAD Synthetase fromBacillus stearothermophilus: Purification, Characterization, Gene Cloning, and Applications

Autor: Issei Yoshioka, Toshihisa Ohshima, Shinji Koga, Haruhhiko Sakuraba, Fumihiko Yamaguchi, Mamori Takahashi

Publikováno v: Bioscience, Biotechnology, and Biochemistry. 66:2052-2059

Bacillus stearothermophilus H-804 isolated from a hot spring in Beppu, Japan, produced an ammonia-specific NAD synthetase (EC 6.3.1.5). The enzyme specifically used NH3 as an amide donor for the synthesis of NAD as it formed AMP and pyrophosphate fro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b7169d7ca265ba381ea037cced1127a
https://doi.org/10.1271/bbb.66.2052

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Increasing the thermostability of Flavobacterium meningosepticum glycerol kinase by changing Ser329 to Asp in the subunit interface region

Autor: Toshihisa Ohshima, Mamoru Takahashi, Hideki Takehara, Hideo Misaki, Haruhiko Sakuraba, Issei Yoshioka, Shin-ichi Sakasegawa, Yoshitaka Kagimoto

Publikováno v: Protein Engineering, Design and Selection. 14:663-667

The thermostability enhancement of Flavobacterium meningosepticum glycerol kinase (FGK) by random mutagenesis in the subunit interface region was investigated. A single Escherichia coli transformant, which produced a more thermostable glycerol kinase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::260c67fadad9aae5e5c433f38f240e5a
https://doi.org/10.1093/protein/14.9.663

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Biochemical Characterization, Cloning, and Sequencing of ADP-Dependent (AMP-Forming) Glucokinase from Two Hyperthermophilic Archaea, Pyrococcus furiosus and Thermococcus litoralis

Autor: Haruhiko Sakuraba, Shinji Koga, Mamoru Takahashi, Issei Yoshioka, Toshihisa Ohshima, Shin-ichi Sakasegawa, Sakayu Shimizu

Publikováno v: Journal of Biochemistry. 128:1079-1085

The ADP-dependent (AMP-forming) glucokinases from the hyperthermophilic archaea Pyrococcus furiosus and Thermococcus litoralis catalyze the phosphorylation of glucose using ADP as the essential phosphoryl group donor. Both enzymes were purified to ho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b1534f6be75002cef799c4937ab09d9
https://doi.org/10.1093/oxfordjournals.jbchem.a022836

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Cloning of a thermostable ascorbate oxidase gene from Acremonium sp. HI-25 and modification of the azide sensitivity of the enzyme by site-directed mutagenesis

Autor: Hideo Misaki, Masashi Kato, Kayoko Takeda, Megumi Yamamoto, Norihiro Tsukagoshi, Sawao Murao, Kengo Shirai, Issei Yoshioka, Sachiko Kajita, Homare Itoh, Takashi Shin

Publikováno v: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1388:444-456

A gene encoding a thermostable ascorbate oxidase (ASOM) was cloned from Acremonium sp. HI-25 and sequenced. The gene comprised 1709 bp and was interrupted by a single intron of 57 bp. ASOM consisted of 551 amino acids including a signal peptide with

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f423b0966bc9c031a302f1eeb14a37f2
https://doi.org/10.1016/s0167-4838(98)00206-4

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Alteration of substrate specificity of fructosyl-amino acid oxidase from Ulocladium sp. JS-103

Autor: Shigeyuki Imamura, Takuji Kouzuma, Jun-ichi Sumitani, Maki Fujiwara, Issei Yoshioka, Motoo Arai, Shinji Koga, Takashi Kawaguchi

Publikováno v: Journal of Bioscience and Bioengineering. 102:241-243

We showed by random mutagenesis that one-amino-acid substitution at Arg94 in fructosyl-amino acid oxidase from Ulocladium sp. JS-103 enhanced substrate specificity toward fructosyl valine (FV), a model compound of hemoglobin A(1c). Kinetic analysis s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b47f236314464b5d11768c270be896df
https://doi.org/10.1263/jbb.102.241

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Cloning and Sequence Analysis of the Gene for Phosphoenolpyruvate Carboxylase from an Extreme Thermophile, Thermus sp1

Autor: Issei Yoshioka, Mamoru Takahashi, Tsutomu Nakamura, Hiroyuki Toh, Katsura Izui

Publikováno v: The Journal of Biochemistry. 118:319-324

The ppc gene, which encodes phosphoenolpyruvate carboxylase (PEPC) of an extreme thermophile, Thermus sp., was cloned and sequenced. The ppc gene had a high G+C content (69.2%). An open reading frame for a 857-amino-acid polypeptide was found in the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::551b88e1ad0346f2a3b4729c328257b9
https://doi.org/10.1093/oxfordjournals.jbchem.a124909

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Phosphoenolpyruvate carboxylase: Alteration of catalytic and regulatory properties by site-directed mutagenesis and isolation of the gene from an extreme thermophile

Autor: Issei Yoshioka, Kazutoyo Terada, Masato Yano, Tsutomu Nakamura, Kunimi Abe, Akio Kihara, Mamoru Takahashi, Katsura Izui

Publikováno v: Energy Conversion and Management. 36:751-754

The roles of several conserved amino acid residues in phosphoenol-pyruvate carboxylase (PEPC, EC4.1.1.31) of E. coli were studied by site-directed mutagenesis. Mutant enzymes H138N (His138 replaced by Asn) and R587S lost the original catalytic activi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::79ab1c7f7b80635a7457bc3ca4ba2ef4
https://doi.org/10.1016/0196-8904(95)00113-r

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Alteration of substrate specificity of fructosyl-amino acid oxidase from Fusarium oxysporum

Autor: Takashi Kawaguchi, Takuji Kouzuma, Shinji Koga, Maki Fujiwara, Motoo Arai, Issei Yoshioka, Jun-ichi Sumitani, Shigeyuki Imamura

Publikováno v: Applied microbiology and biotechnology. 74(4)

Fructosyl-amino acid oxidase (FOD-F) from Fusarium oxysporum f. sp. raphani (NBRC 9972) is the enzyme catalyzing the oxidative deglycation of fructosyl-amino acids such as \( N^{\varepsilon }\)-fructosyl \( N^{\alpha }\)-benzyloxycarbonyl-lysine (FZK

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0c5312ef8a31de6b7e33930d5fc9e46
https://pubmed.ncbi.nlm.nih.gov/17160532

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