Ryo Uehara

Ritsumeikan University

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Kazufumi Takano

Osaka University

Shigenori Kanaya

Osaka University

Yuichi Koga

Osaka University

S. Tanaka

Kagoshima University

Hiroyoshi Matsumura

Ritsumeikan University

Robert J. Crouch

Eunice Kennedy Shriver National Institute of Child Health and Human Development

S. Kanaya

Obayashi (Japan)

Yuichi Koga

Saga-Ken Medical Centre Koseikan

Takuya Yoshizawa

Ritsumeikan University

Hiroshi Amesaka

Kyoto Prefectural University

Cooperative Institutions

Osaka University

Universidade Federal do Rio de Janeiro

National Institutes of Health

Ritsumeikan University

The University of Tokyo

Kyoto University

Instituto de Catálisis y Petroleoquímica

Consejo Superior de Investigaciones Científicas

Universidade Estadual de Maringá

Instituto Nacional de Tecnologia

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Crystal structure of the E496A mutant of HsBglA

Ryo Uehara Reikichi Iwamoto S. Aoki T. Yoshizawa Kazufumi Takano

Crystal (programming language)

10.2210/pdb6m4f/pdb

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Ribonucleotide threshold to induce p53 damage pathway during embryonic development in mouse

Joint Annual Meeting of 51st JSDB and 70th JSCB (2018)

Ryo Uehara

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Requirement of Ca²⁺ Ions for the Hyperthermostability of Tk-Subtilisin from Thermococcus kodakarensis

Biochemistry (2012)

Ryo Uehara Yuki Takeuchi S. Tanaka Kazufumi Takano Yuichi Koga

Tk-subtilisin, a hyperthermostable subtilisin-like serine protease from Thermococcus kodakarensis, matures from the inactive precursor, Pro-Tk-subtilisin (Pro-TKS), upon autoprocessing and degradation of the propeptide (Tkpro). It contains seven Ca2+ ions. Four of them (Ca2–Ca5) are responsible for folding of Tk-subtilisin. In this study, to clarify the role of the other three Ca2+ ions (Ca1, Ca6, and Ca7), we constructed Pro-TKS derivatives lacking the Ca1 ion (Pro-TKS/ΔCa1), Ca6 ion (Pro-TKS/ΔCa6), and Ca7 ion (Pro-TKS/ΔCa7), and their active site mutants (Pro-S324A/ΔCa1, Pro-S324A/ΔCa6, and Pro-S324A/ΔCa7, respectively). Pro-TKS/ΔCa6 and Pro-TKS/ΔCa7 fully matured into their active forms upon incubation at 80 °C for 30 min as did Pro-TKS. The mature enzymes were as active as Tk-subtilisin at 80 °C, indicating that the Ca6 and Ca7 ions are not important for activity. In contrast, Pro-TKS/ΔCa1 matured poorly at 80 °C because of the instability of its mature domain. The enzymatic activity of Tk-subtilisin/ΔCa1 was determined to be 50% of that of Tk-subtilisin using the refolded protein. This result suggests that the Ca1 ion is required for the maximal activity of Tk-subtilisin. The refolding rates of all Pro-S324A derivatives were comparable to that of Pro-S324A (active site mutant of Pro-TKS), indicating that these Ca2+ ions are not needed for folding of Tk-subtilisin. The stabilities of Pro-S324A/ΔCa1 and Pro-S324A/ΔCa6 were decreased by 26.6 and 11.7 °C, respectively, in Tm compared to that of Pro-S324A. The half-lives of Tk-subtilisin/ΔCa6 and Tk-subtilisin/ΔCa7 at 95 °C were 8- and 4-fold lower than that of Tk-subtilisin, respectively. These results suggest that the Ca1, Ca6, and Ca7 ions, especially the Ca1 ion, contribute to the hyperthermostabilization of Tk-subtilisin.

Subtilisin

Protein precursor

Thermococcus

10.1021/bi300427u

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Citations (19)

Hyperthermophilic subtilisin-like proteases from Thermococcus kodakarensis

Elsevier eBooks (2023)

Ryo Uehara Hiroshi Amesaka Yuichi Koga Kazufumi Takano Shigenori Kanaya

Subtilisin

Thermococcus

Protein precursor

Hyperthermophile

10.1016/b978-0-443-19059-9.00003-7

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2P-1100 Tk-subtilisin stabilization mechanism during maturation

日本生物工学会大会講演要旨集 (2010)

Ryo Uehara S. Tanaka Yuichi Koga Kazufumi Takano Shigenori Kanaya

Subtilisin

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Crystal structure of KpFtsZ (residues 11-316)

T. Yoshizawa Jun Fujita H. Terakada Motoyasu Ozawa Natsuki Kuroda

Crystal (programming language)

10.2210/pdb6ll5/pdb

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Unlike the Escherichia coli counterpart, archaeal RNase HII cannot process ribose monophosphate abasic sites and oxidized ribonucleotides embedded in DNA

Journal of Biological Chemistry (2019)

Matilde Clarissa Malfatti Ghislaine Henneke Sathya Balachander Kyung Duk Koh Gary P. Newnam

RNase PH

Ribonucleotide

RNase MRP

RNase H

Ribonucleotide reductase

10.1074/jbc.ra119.009493

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Bone Ingrowth into Ti-Zr Porous Implant and Bone Bonding Strength

日本口腔インプラント学会誌 = Journal of Japanese Society of Oral Implantology (2006)

Ken Niwa Jun Toshina Ryo Uehara Hirotada Koike Toshio Matsuda

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Crystal structure of a GH1 β‐glucosidase from Hamamotoa singularis

Protein Science (2020)

Ryo Uehara Riki Iwamoto Sayaka Aoki Takuya Yoshizawa Kazufumi Takano

A GH1 β-glucosidase from the fungus Hamamotoa singularis (HsBglA) has high transgalactosylation activity and efficiently converts lactose to galactooligosaccharides. Consequently, HsBglA is among the most widely used enzymes for industrial galactooligosaccharide production. Here, we present the first crystal structures of HsBglA with and without 4'-galactosyllactose, a tri-galactooligosaccharide, at 3.0 and 2.1 Å resolutions, respectively. These structures reveal details of the structural elements that define the catalytic activity and substrate binding of HsBglA, and provide a possible interpretation for its high catalytic potency for transgalactosylation reaction.

Crystal (programming language)

10.1002/pro.3916

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Crystal structure of Pro-S324A/D356A

Ryo Uehara Clement Angkawidjaja Yuichi Koga S. Kanaya

10.2210/pdb3wiu/pdb

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