Zobrazeno 1 - 10
of 49
pro vyhledávání: '"Hitoshi Kusakabe"'
Autor:
Masaki Kitagawa, Nanako Ito, Yuya Matsumoto, Masaya Saito, Takashi Tamura, Hitoshi Kusakabe, Kenji Inagaki, Katsumi Imada
Publikováno v:
Journal of Structural Biology: X, Vol 5, Iss , Pp 100044- (2021)
Harmuful proteins are usually synthesized as inactive precursors and are activated by proteolytic processing. l-Amino acid oxidase (LAAO) is a flavoenzyme that catalyzes the oxidative deamination of l-amino acid to produce a 2-oxo acid with ammonia a
Externí odkaz:
https://doaj.org/article/5f0a8e4c2a224ee8be3aba411458a521
Autor:
Hitoshi KUSAKABE
Publikováno v:
KAGAKU TO SEIBUTSU. 59:520-526
Autor:
Takashi Tamura, Yuya Matsumoto, Katsumi Imada, Shigeru Sugiyama, Kenji Inagaki, Masaya Saito, Marie Amano, Hiroki Kondo, Hitoshi Kusakabe, Masaki Kitagawa
Publikováno v:
Protein Sci
l‐Lysine oxidase (LysOX) is a FAD‐dependent homodimeric enzyme that catalyzes the oxidative deamination of l‐lysine to produce α‐keto‐ε‐aminocaproate with ammonia and hydrogen peroxide. LysOX shows strict substrate specificity for l‐l
Autor:
Kenji Inagaki, Katsumi Imada, Yoshika Yano, Nanako Ito, Hitoshi Kusakabe, Shinsaku Matsuo, Takashi Tamura
Publikováno v:
Protein Sci
The alternation of substrate specificity expands the application range of enzymes in industrial, medical, and pharmaceutical fields. l-Glutamate oxidase (LGOX) from Streptomyces sp. X-119-6 catalyzes the oxidative deamination of l-glutamate to produc
Autor:
Kenji Inagaki, Takashi Tamura, Masaya Saito, Masaki Kitagawa, Yuya Matsumoto, Hitoshi Kusakabe, Katsumi Imada, Nanako Ito
Publikováno v:
Journal of Structural Biology: X, Vol 5, Iss, Pp 100044-(2021)
Journal of Structural Biology: X
Journal of Structural Biology: X
Graphical abstract
Highlights • The suppression mechanism of activity by propeptide remains unclear for most LAAOs. • The crystal structures of the LysOX precursor (prLysOX) have been determined. • The propeptide indirectly changes the act
Highlights • The suppression mechanism of activity by propeptide remains unclear for most LAAOs. • The crystal structures of the LysOX precursor (prLysOX) have been determined. • The propeptide indirectly changes the act
Publikováno v:
Bioscience, biotechnology, and biochemistry. 84(1)
We developed an enzymatic assay system enabling easy quantification of 4-aminobutyric acid (GABA). The reaction of GABA aminotransferase obtained from Streptomyces decoyicus NBRC 13977 was combined to those of the previously developed glutamate assay
Autor:
Katsumi Imada, Takashi Tamura, Kenji Inagaki, Marie Amano, Junko Inagaki, Hiroki Kondo, Tatsuya Kawaguchi, Hitoshi Kusakabe, Tadahisa Sano, Haruka Mizuguchi, Kengo Shinyashiki
Publikováno v:
Journal of Biochemistry. 157:549-559
L-Lysine α-oxidase (LysOX) from Trichoderma viride is a homodimeric 112 kDa flavoenzyme that catalyzes the oxidative deamination of L-lysine to form α-keto-ε-aminocaproate. LysOX severely inhibited growth of cancer cells but showed relatively low
Publikováno v:
Proceedings of the National Academy of Sciences. 111:17152-17157
Organocatalysts, low-molecular mass organic compounds composed of nonmetallic elements, are often used in organic synthesis, but there have been no reports of organocatalysts of biological origin that function in vivo. Here, we report that actinorhod
Publikováno v:
Bioscience, biotechnology, and biochemistry. 63(12)
We studied production of D-glutamate from L-glutamate using a bioreactor consisting of two columns of sequentially connected immobilized glutamate racemase (EC 5.1.1.3, from Bacillus subtilis IFO 3336) and L-glutamate oxidase (EC 1.4.3.11, from Strep
Autor:
Shigetoshi Sugio, Hitoshi Kusakabe, Akiko Kashima, Takashi Tamura, Hiroshi Mizuno, Chiduko Sasaki, Chika Sakaguchi, Jiro Arima, Kenji Inagaki
Publikováno v:
FEBS Journal. 276:3894-3903
L-Glutamate oxidase (LGOX) from Streptomyces sp. X-119-6, which catalyzes the oxidative deamination of L-glutamate, has attracted increasing attention as a component of amperometric L-glutamate sensors used in the food industry and clinical biochemis