His main research concerns Biochemistry, Peptide sequence, Stereochemistry, Enzyme and Amino acid. His work investigates the relationship between Biochemistry and topics such as Anthocyanin that intersect with problems in Complementary DNA. He has included themes like Acyltransferases, Tyrosinase, Alanine, Binding site and Histidine in his Stereochemistry study.
His Enzyme study combines topics in areas such as Residue and Isoflavonoid. His study looks at the intersection of Amino acid and topics like Farnesyl diphosphate synthase with Prenylation. His research integrates issues of Plasmid and Prenyltransferase in his study of Escherichia coli.
His primary areas of investigation include Biochemistry, Stereochemistry, Enzyme, ATP synthase and Amino acid. Peptide sequence, Mutant, Prenyltransferase, Escherichia coli and Gene are the subjects of his Biochemistry studies. His biological study deals with issues like Substrate, which deal with fields such as Micrococcus luteus.
His work focuses on many connections between Enzyme and other disciplines, such as Molecular cloning, that overlap with his field of interest in Nucleic acid sequence. His ATP synthase study integrates concerns from other disciplines, such as Sulfolobus acidocaldarius and Sulfolobus solfataricus. His Amino acid research incorporates themes from Tyrosine, Amino acid residue and Serine.
Tokuzo Nishino mainly investigates Biochemistry, Stereochemistry, Enzyme, Amino acid and Anthocyanin. His Biochemistry course of study focuses on Bacteria and Microbiology. He has researched Stereochemistry in several fields, including Isomerase, Chalcone synthase, Sulfolobus shibatae and Active site.
His study in Escherichia coli extends to Enzyme with its themes. His Amino acid research is multidisciplinary, incorporating perspectives in Glycyrrhiza echinata, Enzyme catalysis and Residue. His Anthocyanin study incorporates themes from Protein structure and Binding site.
Tokuzo Nishino mostly deals with Biochemistry, Enzyme, Stereochemistry, Biosynthesis and Isoflavonoid. His research brings together the fields of Genistein and Biochemistry. Many of his research projects under Enzyme are closely connected to Membrane lipids with Membrane lipids, tying the diverse disciplines of science together.
His Stereochemistry study combines topics from a wide range of disciplines, such as Reducing agent, Cofactor, Flavin group, Redox and NAD+ kinase. His Isoflavonoid research includes themes of Amino acid, Enzyme catalysis, Glycyrrhiza echinata and Residue. His research investigates the link between Acyltransferases and topics such as Binding site that cross with problems in Peptide sequence.
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Aureusidin Synthase: A Polyphenol Oxidase Homolog Responsible for Flower Coloration
T. Nakayama;K. Yonekura-Sakakibara;T. Sato;S. Kikuchi.
Science (2000)
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.
Journal of Biological Chemistry (1996)
Thermostable Farnesyl Diphosphate Synthase of Bacillus stearothermophilus: Molecular Cloning, Sequence Determination, Overproduction, and Purification.
Tanetoshi Koyama;Shusei Obata;Masami Osabe;Ayumi Takeshita.
Journal of Biochemistry (1993)
Cloning and nucleotide sequence of the ispA gene responsible for farnesyl diphosphate synthase activity in Escherichia coli.
Shingo Fujisaki;Hiroshi Hara;Yukinobu Nishimura;Kensuke Horiuchi.
Journal of Biochemistry (1990)
Conversion of Product Specificity of Archaebacterial Geranylgeranyl-diphosphate Synthase: IDENTIFICATION OF ESSENTIAL AMINO ACID RESIDUES FOR CHAIN LENGTH DETERMINATION OF PRENYLTRANSFERASE REACTION *
Shin-ichi Ohnuma;Kazutake Hirooka;Hisashi Hemmi;Chika Ishida.
Journal of Biological Chemistry (1996)
Conversion from Farnesyl Diphosphate Synthase to Geranylgeranyl Diphosphate Synthase by Random Chemical Mutagenesis
Shin-ichi Ohnuma;Takeshi Nakazawa;Hisashi Hemmi;Anna-Maria Hallberg.
Journal of Biological Chemistry (1996)
Archaebacterial ether-linked lipid biosynthetic gene. Expression cloning, sequencing, and characterization of geranylgeranyl-diphosphate synthase.
Shin-Ichi Ohnuma;Manabu Suzuki;Tokuzo Nishino.
Journal of Biological Chemistry (1994)
A UDP-glucose:isoflavone 7-O-glucosyltransferase from the roots of soybean (glycine max) seedlings. Purification, gene cloning, phylogenetics, and an implication for an alternative strategy of enzyme catalysis.
Akio Noguchi;Atsushi Saito;Yu Homma;Masahiro Nakao.
Journal of Biological Chemistry (2007)
Cold-active esterase from Psychrobacter sp. Ant300: gene cloning, characterization, and the effects of Gly→Pro substitution near the active site on its catalytic activity and stability
Ljudmila Kulakova;Andrey Galkin;Toru Nakayama;Tokuzo Nishino.
Biochimica et Biophysica Acta (2004)
Polyprenyl diphosphate synthase essentially defines the length of the side chain of ubiquinone
Kazunori Okada;Kengo Suzuki;Yasuhiro Kamiya;XuFen Zhu.
Biochimica et Biophysica Acta (1996)
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