Y
Yasuhisa Fukuta
Researcher at Toyama Prefectural University
Publications - 9
Citations - 141
Yasuhisa Fukuta is an academic researcher from Toyama Prefectural University. The author has contributed to research in topics: Gene & Enzyme. The author has an hindex of 7, co-authored 7 publications receiving 129 citations.
Papers
More filters
Journal ArticleDOI
Characterization of a New (R)-Hydroxynitrile Lyase from the Japanese Apricot Prunus mume and cDNA Cloning and Secretory Expression of One of the Isozymes in Pichia pastoris
Yasuhisa Fukuta,Samik Nanda,Yasuo Kato,Hiroya Yurimoto,Yasuyoshi Sakai,Hidenobu Komeda,Yasuhisa Asano +6 more
TL;DR: PmHNL, a hydroxynitrile lyase from Japanese apricot ume (Prunus mume) seed was purified to homogeneity by ammonium sulfate fractionation and chromatographic steps and the deduced amino acid sequence was found to be highly similar to that of an enzyme from Pr.
Journal ArticleDOI
The Screening, Characterization, and Use of ω-Laurolactam Hydrolase : A New Enzymatic Synthesis of 12-Aminolauric Acid
TL;DR: Several ω-laurolactam degrading microorganisms were isolated from soil samples and the deduced amino acid sequence showed high homology with 6-aminohexanoate-cyclic-dimer hydrolase (EC 3.5.2.12) from Arthrobacter sp.
Journal ArticleDOI
Purification and characterization of an L-amino acid oxidase from Pseudomonas sp. AIU 813.
TL;DR: An L-amino acid oxidase was found from a newly isolated strain, Pseudomonas sp.
Journal ArticleDOI
Mutational and crystallographic analysis of l-amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813: Interconversion between oxidase and monooxygenase activities.
Daisuke Matsui,Do-Hyun Im,Asami Sugawara,Yasuhisa Fukuta,Shinya Fushinobu,Kimiyasu Isobe,Yasuhisa Asano +6 more
TL;DR: A high‐resolution three‐dimensional structure of l‐AAO/MOG is determined to provide a structural basis for its biochemical characteristics and it is suggested that a slight difference of the binding position of a substrate can dictate the activity of this type of enzyme as oxidase or monooxygenase.