Výsledky vyhledávání - "Terutaka Yazaki"

Identification of Regions Critically Affecting Kinetics and Allosteric Regulation of the Escherichia coli ADP-Glucose Pyrophosphorylase by Modeling and Pentapeptide-Scanning Mutagenesis

Autor: Esteban Erben, Ana L. Bertolo, Corina M. Fusari, Carlos Maria Figueroa, Alberto A. Iglesias, Jennifer R. Schmidt, Jack Preiss, Terutaka Yazaki, Mabel Cristina Aleanzi, Clarisa M. Bejar, Miguel A. Ballicora, Ana María Magdalena Demonte

Publikováno v: Journal of Bacteriology. 189:5325-5333

ADP-glucose pyrophosphorylase (ADP-Glc PPase) is the enzyme responsible for the regulation of bacterial glycogen synthesis. To perform a structure-function relationship study of the Escherichia coli ADP-Glc PPase enzyme, we studied the effects of pen

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92362275dfebc99321ea2f079bd26109
https://doi.org/10.1128/jb.00481-07

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A Microbial Sensor for Highly Sensitive and Automatic Determination of Sulfite in Foods and Food Materials. Kinetic Study of the Sulfite Dehydrogenase-catalyzed Reaction in the Microbial State of Thiobacillus thiooxidans

Autor: Takashi Matsumoto, Masatake Ohnishi, Terutaka Yazaki

Publikováno v: Journal of Applied Glycoscience. 47:169-175

A highly sensitive and automatic microbial sensor apparatus has been constructed with Thiobacillus thiooxidans and employed for sulfite analysis of food materials in practical fields including the starch industry, thus we tried to obtain enzymatic ba

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2766d0b394c63da7a347e15d9aececea
https://doi.org/10.5458/jag.47.169

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Characterization of the subsite structure of the β-glucosidase from Aspergillus niger, an aspect of the mechanism of carbohydrate recognition11Presented in part at the Annual Meeting of the Japan Society for Glycoscience (Oyo Toshitsu-kagaku), Tsukuba, Japan 1996

Autor: Terutaka Yazaki, Gentaro Okada, Masatake Ohnishi

Publikováno v: Carbohydrate Research. 308:201-205

Steady-state kinetics on the reaction catalyzed by the β -glucosidase of Aspergillus niger were carried out to evaluate the kinetic parameters, K m and k o , for phenyl β - d -glucosides. The k o /K m values, which may relate to productive binding

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0e6e313b1c44ddd65cf893305934543b
https://doi.org/10.1016/s0008-6215(98)00025-1

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Subsite structure of the β-glucosidase from Aspergillus niger, evaluated by steady-state kinetics with cello-oligosaccharides as substrates

Autor: Gentaro Okada, Masatake Ohnishi, Souji Rokushika, Terutaka Yazaki

Publikováno v: Carbohydrate Research. 298:51-57

The β-glucosidase from a commercially available preparation from Aspergillus niger was highly purified. The Michaelis constant K m and the molar activity k 0 for cello-oligosaccharide substrates G n ( n = 2–6) were obtained by steady-state kinetic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1368008181ae32f356ce4c59a9d79136
https://doi.org/10.1016/s0008-6215(96)00287-x

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High Recovery Purification and Some Properties of aβ-Glucosidase fromAspergillus niger

Autor: Yoshimasa Tanaka, Teruo Nakakuki, Takehiro Unno, Gentaro Okada, Terutaka Yazaki, Katsutoshi Ide

Publikováno v: Bioscience, Biotechnology, and Biochemistry. 57:2172-2173

A β-glucosidase was intensively purified with high recovery from a commercial preparation of Aspergillus niger by consecutive column chromatography. The enzyme was an acidic protein with a pI of 3.8, and split cellotriose to produce specifically β-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d908480f2d5d2bac783d209639ac13ef
https://doi.org/10.1271/bbb.57.2172

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