M
Masahiro Takeo
Researcher at University of Hyogo
Publications - 103
Citations - 1486
Masahiro Takeo is an academic researcher from University of Hyogo. The author has contributed to research in topics: Hydrolase & Pseudomonas putida. The author has an hindex of 21, co-authored 95 publications receiving 1283 citations.
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Journal ArticleDOI
Degradation of 4-Nitrophenol, 2-Chloro-4-nitrophenol, and 2,4-Dinitrophenol by Rhodococcus imtechensis Strain RKJ300
Anuradha Ghosh,Meenu Khurana,Archana Chauhan,Masahiro Takeo,Asit K. Chakraborti,Rakesh K. Jain +5 more
TL;DR: Lab-scale soil microcosm studies demonstrated that the organism was capable of degrading a mixture of nitrophenols simultaneously, indicating its applicability toward in situ bioremediation of contaminated sites.
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Plasmid-encoded genes specifying aniline oxidation from Acinetobacter sp. strain YAA.
TL;DR: Results suggest that in strain YAA aniline is degraded via catechol through a pathway involving meta-cleavage of the benzene-ring by plasmid-encoded genes including atdA.
Journal ArticleDOI
Mechanism of 4-Nitrophenol Oxidation in Rhodococcus sp. Strain PN1: Characterization of the Two-Component 4-Nitrophenol Hydroxylase and Regulation of Its Expression
Masahiro Takeo,Masumi Murakami,Sanae Niihara,Kenta Yamamoto,Munehiro Nishimura,Dai-ichiro Kato,Seiji Negoro +6 more
TL;DR: Functional analysis, in addition to the sequence analysis, revealed that the 4-NP hydroxylase system belongs to the two-component flavin-diffusible monooxygenase family.
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Chromosome-encoded gene cluster for the metabolic pathway that converts aniline to TCA-cycle intermediates in Delftia tsuruhatensis AD9
TL;DR: Results suggest that, in strain AD9, aniline is degraded via catechol through a meta-cleavage pathway by the chromosome-encoded tad gene cluster.
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Nylon-oligomer degrading enzyme/substrate complex: catalytic mechanism of 6-aminohexanoate-dimer hydrolase
Seiji Negoro,Taku Ohki,Naoki Shibata,Kazuhiro Sasa,Haruhisa Hayashi,Hidehiko Nakano,Kengo Yasuhira,Dai-ichiro Kato,Masahiro Takeo,Yoshiki Higuchi +9 more
TL;DR: It is proposed here that the enzyme catalysis proceeds according to the following steps: Ald-induced transition from open to closed form, nucleophilic attack of Ser112 to Ald and formation of a tetrahedral intermediate, formation of acyl enzyme and transition to open form, and deacylation.