T
Tatsuo Kurihara
Researcher at Kyoto University
Publications - 181
Citations - 5448
Tatsuo Kurihara is an academic researcher from Kyoto University. The author has contributed to research in topics: Dehalogenase & Selenocysteine. The author has an hindex of 42, co-authored 174 publications receiving 5101 citations. Previous affiliations of Tatsuo Kurihara include University of California, Berkeley & University of Łódź.
Papers
More filters
Journal ArticleDOI
A Cold-Adapted Lipase of an Alaskan Psychrotroph,Pseudomonas sp. Strain B11-1: Gene Cloning and Enzyme Purification and Characterization
TL;DR: The enzyme showed a 1,3-positional specificity toward triolein and was stable between pH 6 and 9, and the optimal pH for the enzymatic hydrolysis of tributyrin was around 8.2, while the enzyme was unstable at temperatures higher than 45°C.
Journal ArticleDOI
Cysteine sulfinate desulfinase, a nifs-like protein of escherichia coli with selenocysteine lyase and cysteine desulfurase activities : gene cloning, purification, and characterization of a novel pyridoxal enzyme
TL;DR: Zheng et al. as discussed by the authors proposed a new enzyme called cysteine sulfinate desulfinase (Cys-SDS), which is distinct from A. vinelandii NIFS.
Journal ArticleDOI
Lst1p and Sec24p Cooperate in Sorting of the Plasma Membrane Atpase into Copii Vesicles in Saccharomyces cerevisiae
TL;DR: Results suggest that Lst1p and Sec24p cooperate in the packaging of Pma1p, the essential plasma membrane ATPase, and support the view that biosynthetic precursors of plasma membrane proteins must be sorted into ER-derived transport vesicles.
Journal ArticleDOI
Crystal Structure of L-2-Haloacid Dehalogenase from Pseudomonas sp. YL: AN α/β HYDROLASE STRUCTURE THAT IS DIFFERENT FROM THE α/β HYDROLASE FOLD
TL;DR: The structure of the homodimeric enzyme from Pseudomonas sp. YL has been determined by a multiple isomorphous replacement method and refined at 2.5 A resolution to a crystallographic R-factor of 19.5%.
Journal ArticleDOI
Characterization of a NifS-like chloroplast protein from Arabidopsis. Implications for its role in sulfur and selenium metabolism.
Elizabeth A. H. Pilon-Smits,Gulnara F. Garifullina,Salah E. Abdel-Ghany,Shin-ichiro Kato,Hisaaki Mihara,Kerry L. Hale,Jason L. Burkhead,Nobuyoshi Esaki,Tatsuo Kurihara,Marinus Pilon +9 more
TL;DR: The goal of these studies was to identify and characterize chloroplast NifS-like proteins, and the possible role of AtCpNifS in plastidic Fe-S cluster formation or in Se metabolism is discussed.