Výsledky vyhledávání - "Evans Menach"

Effects of Conversion of the Zinc-Binding Motif Sequence of Thermolysin, HEXXH, to That of Dipeptidyl Peptidase III, HEXXXH, on the Activity and Stability of Thermolysin

Autor: Kuniyo Inouye, Evans Menach, Kiyoshi Yasukawa, Yasuhiko Hashida

Publikováno v: Bioscience, Biotechnology, and Biochemistry. 77:1901-1906

Most zinc metalloproteinases have the consensus zinc-binding motif sequence HEXXH, in which two histidine residues chelate a catalytic zinc ion. The zinc-binding motif sequence of thermolysin, H(142)ELTH(146), belongs to this motif sequence, while th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::efd75cd2fc6960658d65b6c9979432a6
https://doi.org/10.1271/bbb.130360

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Effects of Mutations of Thermolysin, Asn116 to Asp and Asp150 to Glu, on Salt-Induced Activation and Stabilization

Autor: Kuniyo Inouye, Evans Menach, Kiyoshi Yasukawa

Publikováno v: Bioscience, Biotechnology, and Biochemistry. 77:741-746

Neutral salts activate and stabilize thermolysin. We previously found that two single mutations, Asn116→Asp and Asp150→Glu, increase the activity of thermolysin. In the present study, we examined their effects on NaCl-induced activation and stabi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef9b9539c791d5bf85f883687e6a0050
https://doi.org/10.1271/bbb.120865

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Effects of site-directed mutagenesis of Asn116 in the -hairpin of the N-terminal domain of thermolysin on its activity and stability

Autor: Kuniyo Inouye, Kiyoshi Yasukawa, Evans Menach

Publikováno v: Journal of Biochemistry. 152:231-239

In the N-terminal domain of thermolysin, two anti-parallel β-strands, Asn112-Ala113-Phe114-Trp115 and Ser118-Gln119-Met120-Val121-Tyr122 are connected by an Asn116-Gly117 turn to form a β-hairpin structure. In this study, we examined the role of As

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f0b36372824826f42e98c9749097282
https://doi.org/10.1093/jb/mvs064

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Effects of Site-Directed Mutagenesis of the Loop Residue of the N-Terminal Domain Gly117 of Thermolysin on Its Catalytic Activity

Autor: Kiyoshi Yasukawa, Evans Menach, Kuniyo Inouye

Publikováno v: Bioscience, Biotechnology, and Biochemistry. 74:2457-2462

In the N-terminal domain of thermolysin, two polypeptide strands, Asn112-Ala113-Phe114-Trp115 and Ser118-Gln119-Met120-Val121-Tyr122, are connected by a short loop, Asn116-Gly117, to form an anti-parallel β-sheet. The Asn112-Trp115 strand is located

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94d8459bf035e4001879937f5d258836
https://doi.org/10.1271/bbb.100536

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