Hidehiko Kumagai mainly investigates Biochemistry, Enzyme, Stereochemistry, Escherichia coli and Amino acid. His research on Biochemistry frequently connects to adjacent areas such as Molecular biology. His studies in Enzyme integrate themes in fields like Bifidobacterium longum, Mutant and Transcriptional regulation.
His work deals with themes such as Hydrolase and Protein structure, which intersect with Stereochemistry. The various areas that Hidehiko Kumagai examines in his Escherichia coli study include Putrescine, Hydrolysis and Glutathione. His study in Amino acid is interdisciplinary in nature, drawing from both Lymphocyte cytosolic protein 2, Microbial transformation, G protein-coupled receptor and Molecular mass.
His primary areas of investigation include Biochemistry, Enzyme, Stereochemistry, Escherichia coli and Chromatography. His Biochemistry research is multidisciplinary, incorporating perspectives in Molecular biology and Bacteria. The concepts of his Bacteria study are interwoven with issues in Fermentation and Microbiology.
Enzyme is closely attributed to Hydrolysis in his work. His Stereochemistry study incorporates themes from Residue, Hydrolase, Substrate, Glutamine and Tyrosine phenol-lyase. The Residue study combines topics in areas such as Oligosaccharide and Peptide.
His primary areas of study are Biochemistry, Enzyme, Stereochemistry, Escherichia coli and Fermentation. His works in Benzylisoquinoline, Glycoside hydrolase, Amino acid, Peptide sequence and Metabolic engineering are all subjects of inquiry into Biochemistry. Hidehiko Kumagai combines subjects such as Mutagenesis, Mutant, Gene and Tyrosine with his study of Enzyme.
His biological study spans a wide range of topics, including Hydrolase, Bifidobacterium longum, Protein structure and Substrate. His Escherichia coli study combines topics from a wide range of disciplines, such as Morphine, Putrescine and Bacillus subtilis. His Fermentation study combines topics in areas such as Yeast, Cellobiose, Microbiology and Bacteria.
His primary scientific interests are in Biochemistry, Enzyme, Stereochemistry, Glycoside hydrolase and Escherichia coli. His Biochemistry study frequently links to related topics such as Bacteria. His research investigates the connection with Bacteria and areas like Secondary metabolism which intersect with concerns in Benzylisoquinoline.
His Enzyme research includes themes of Organism, Genetics, Lactose and Genome. His work carried out in the field of Stereochemistry brings together such families of science as Hydrolase, Protein structure and Mutant. His study focuses on the intersection of Escherichia coli and fields such as Amino acid with connections in the field of DNA ligase, Putrescine, Molecular mass and Moiety.
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Physiology of Consumption of Human Milk Oligosaccharides by Infant Gut-associated Bifidobacteria
Sadaki Asakuma;Emi Hatakeyama;Tadasu Urashima;Erina Yoshida.
Journal of Biological Chemistry (2011)
Microbial production of plant benzylisoquinoline alkaloids
Hiromichi Minami;Ju-Sung Kim;Nobuhiro Ikezawa;Tomoya Takemura.
Proceedings of the National Academy of Sciences of the United States of America (2008)
Tyrosine Phenol Lyase I. PURIFICATION, CRYSTALLIZATION, AND PROPERTIES
Hidehiko Kumagai;Hideaki Yamada;Hiroshi Matsui;Haruyuki Ohkishi.
Journal of Biological Chemistry (1970)
Molecular Cloning and Characterization of Bifidobacterium bifidum 1,2-α-l-Fucosidase (AfcA), a Novel Inverting Glycosidase (Glycoside Hydrolase Family 95)
Takane Katayama;Akiko Sakuma;Takatoshi Kimura;Yutaka Makimura.
Journal of Bacteriology (2004)
A bacterial platform for fermentative production of plant alkaloids
Akira Nakagawa;Hiromichi Minami;Ju-Sung Kim;Ju-Sung Kim;Takashi Koyanagi.
Nature Communications (2011)
gamma-Glutamyltranspeptidase from Escherichia coli K-12: purification and properties.
H Suzuki;H Kumagai;T Tochikura.
Journal of Bacteriology (1986)
Two distinct α-l-fucosidases from Bifidobacterium bifidum are essential for the utilization of fucosylated milk oligosaccharides and glycoconjugates
Hisashi Ashida;Akiko Miyake;Masashi Kiyohara;Jun Wada.
Bifidobacterium bifidum Lacto-N-Biosidase, a Critical Enzyme for the Degradation of Human Milk Oligosaccharides with a Type 1 Structure
Jun Wada;Jun Wada;Takuro Ando;Masashi Kiyohara;Hisashi Ashida.
Applied and Environmental Microbiology (2008)
Distribution of Hydantoin Hydrolyzing Activity in Microorganisms : Microbial Transformation of Hydantoins to Amino Acids(I) :
Hideaki Yamada;Satomi Takahashi;Yoshiaki Kii;Hidehiko Kumagai.
Journal of Fermentation Technology (1978)
Crystal structures of γ-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate
Toshihiro Okada;Hideyuki Suzuki;Kei Wada;Hidehiko Kumagai.
Proceedings of the National Academy of Sciences of the United States of America (2006)
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