T
Tokuzo Nishino
Researcher at Tohoku University
Publications - 164
Citations - 5316
Tokuzo Nishino is an academic researcher from Tohoku University. The author has contributed to research in topics: Prenyltransferase & ATP synthase. The author has an hindex of 42, co-authored 164 publications receiving 5050 citations. Previous affiliations of Tokuzo Nishino include Yamagata University & Toyota.
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Journal ArticleDOI
Aureusidin Synthase: A Polyphenol Oxidase Homolog Responsible for Flower Coloration
Toru Nakayama,Keiko Yonekura-Sakakibara,Takafumi Sato,S. Kikuchi,Yuko Fukui,Masako Fukuchi-Mizutani,Takashi Ueda,Masahiro Nakao,Yoshikazu Tanaka,Takaaki Kusumi,Tokuzo Nishino +10 more
TL;DR: DNA sequence analysis revealed that aureusidin synthase belongs to the plant polyphenol oxidase family, providing an unequivocal example of the function of the polyphenl oxidase homolog in plants, i.e., flower coloration.
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Conversion from Farnesyl Diphosphate Synthase to Geranylgeranyl Diphosphate Synthase by Random Chemical Mutagenesis
Shin-ichi Ohnuma,Takeshi Nakazawa,Hisashi Hemmi,Anna-Maria Hallberg,Tanetoshi Koyama,Kyozo Ogura,Tokuzo Nishino +6 more
TL;DR: Comparisons of kinetic parameters of the mutated and wild type enzymes revealed several phenomena that may relate with the change of the ultimate chain length, which might suggest that the aromatic ring of tyrosine 81 blocks the chain elongation longer than FPP.
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A Role of the Amino Acid Residue Located on the Fifth Position before the First Aspartate-rich Motif of Farnesyl Diphosphate Synthase on Determination of the Final Product
Shin-ichi Ohnuma,Keishi Narita,Takeshi Nakazawa,Chika Ishida,Yoshie Takeuchi,Chikara Ohto,Tokuzo Nishino +6 more
TL;DR: 20 FPP synthases, each of which has a different amino acid at position 81, are constructed and analyzed, and observations strongly indicate that the amino acid does not come into contact with the substrates but directly contacts the ω-terminal of an elongating allylic product.
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Cloning and nucleotide sequence of the ispA gene responsible for farnesyl diphosphate synthase activity in Escherichia coli.
TL;DR: The molecular cloning and the determination of the nucleotide sequence of the ispA gene responsible for farnesyl diphosphate (FPP) synthase [EC 2.5.1.1] activity in Escherichia coli are described.
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Thermostable Farnesyl Diphosphate Synthase of Bacillus stearothermophilus: Molecular Cloning, Sequence Determination, Overproduction, and Purification.
Tanetoshi Koyama,Shusei Obata,Masami Osabe,Ayumi Takeshita,Ken Yokoyama,Masatoshi Uchida,Tokuzo Nishino,Kyozo Ogura +7 more
TL;DR: The structural gene for thermostable farnesyl diphosphate synthase from Bacillus stearothermophilus was cloned, sequenced, and overexpressed in Escherichia coli cells and the deduced amino acid sequence shows a 42% similarity with that of E. coli FPP synthase.