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186 results on '"Ano, Yoshitaka"'

1. Characterization of a cryptic, pyrroloquinoline quinone-dependent dehydrogenase of Gluconobacter sp. strain CHM43

Author

Nguyen, Thuy Minh, Naoki, Kotone, Kataoka, Naoya, Matsutani, Minenosuke, Ano, Yoshitaka, Adachi, Osao, Matsushita, Kazunobu, and Yakushi, Toshiharu

Subjects
Biochemistry and Cell Biology, Crop and Pasture Production, Biotechnology, Biochemistry and cell biology, Industrial biotechnology, Microbiology
Abstract

ABSTRACT: We characterized the pyrroloquinoline quinone (PQQ)-dependent dehydrogenase 9 (PQQ-DH9) of Gluconobacter sp. strain CHM43, which is a homolog of PQQ-dependent glycerol dehydrogenase (GLDH). We used a plasmid construct to express PQQ-DH9. The expression host was a derivative strain of CHM43, which lacked the genes for GLDH and the membrane-bound alcohol dehydrogenase and consequently had minimal ability to oxidize primary and secondary alcohols. The membranes of the transformant exhibited considerable d-arabitol dehydrogenase activity, whereas the reference strain did not, even if it had PQQ-DH9-encoding genes in the chromosome and harbored the empty vector. This suggests that PQQ-DH9 is not expressed in the genome. The activities of the membranes containing PQQ-DH9 and GLDH suggested that similar to GLDH, PQQ-DH9 oxidized a wide variety of secondary alcohols but had higher Michaelis constants than GLDH with regard to linear substrates such as glycerol. Cyclic substrates such as cis-1,2-cyclohexanediol were readily oxidized by PQQ-DH9.

Published
2021

7. Histamine elimination by a coupling reaction of fungal amine oxidase and bacterial aldehyde oxidase

Author

Usui, Masakatsu, primary, Kubota, Hikari, additional, Ishihara, Mizuki, additional, Matsuki, Haruka, additional, Kawabe, Shinya, additional, Sugiura, Yoshimasa, additional, Kataoka, Naoya, additional, Matsushita, Kazunobu, additional, Ano, Yoshitaka, additional, Akakabe, Yoshihiko, additional, Hours, Roque A, additional, Yakushi, Toshiharu, additional, and Adachi, Osao, additional

Published
2022
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13. Pl4P-signaling pathway for the synthesis of a nascent membrane structure in selective autophagy

Author

Yamashita, Shun-ichi, Oku, Masahide, Wasada, Yuko, Ano, Yoshitaka, and Sakai, Yasuyoshi

Subjects
Phagocytes -- Research, Membranes (Biology) -- Research, Phosphoinositides -- Research, Biological sciences
Abstract

Phosphoinositides regulate a wide range of cellular activities, including membrane trafficking and biogenesis, via interaction with various effector proteins that contain phosphoinositide binding motifs. We show that in the yeast Pichia pastoris, phosphatidylinositol 4'-monophosphate (Pl4P) initiates de novo membrane synthesis that is required for peroxisome degradation by selective autophagy and that this Pl4P signaling is modulated by an ergosterol-converting PpAtg26 (autophagy-related) protein harboring a novel Pl4P binding GRAM (glucosyltransferase, Rab-like GTPase activators, and myotubularins) domain. A phosphatidylinositol-4-OH kinase, PpPik1, is the primary source of Pl4P. Pl4P concentrated in a protein-lipid nucleation complex recruits PpAtg26 through an interaction with the GRAM domain. Sterol conversion by PpAtg26 at the nucleation complex is necessary for elongation and maturation of the membrane structure. This study reveals the role of the Pl4P-signaling pathway in selective autophagy, a process comprising multistep molecular events that lead to the de novo membrane formation.

Published
2006

16. Periplasmic dehydroshikimate dehydratase combined with quinate oxidation in Gluconobacter oxydansfor protocatechuate production

Author

Nagaki, Kakeru, Kataoka, Naoya, Theeragool, Gunjana, Matsutani, Minenosuke, Ano, Yoshitaka, Matsushita, Kazunobu, and Yakushi, Toshiharu

Abstract

Protocatechuate (3,4-dihydroxybenzoate) has antioxidant properties and is a raw material for the production of muconic acid, which is a key compound in the synthesis of polymers such as nylon and polyethylene terephthalate. Gluconobacter oxydansstrain NBRC3244 has a periplasmic system for oxidation of quinate to produce 3-dehydroquinate. Previously, a periplasmic 3-dehydroshikimate production system was constructed by heterologously expressing Gluconacetobacter diazotrophicusdehydroquinate dehydratase in the periplasm of G. oxydansstrain NBRC3244. 3-Dehydroshikimate is converted to protocatechuate by dehydration. In this study, we constructed a G. oxydansstrain that expresses the Acinetobacter baylyi quiCgene, which encodes a dehydroshikimate dehydratase of which the subcellular localization is likely the periplasm. We attempted to produce protocatechuate by co-cultivation of two recombinant G. oxydansstrains—one expressing the periplasmically targeted dehydroquinate dehydratase and the other expressing A. baylyidehydroshikimate dehydratase. The co-cultivation system produced protocatechuate from quinate in a nearly quantitative manner.Graphical AbstractPeriplasmic metabolic engineering in Gluconobactersp. to expand the intrinsic quinate oxidation to protocatechuate production by heterologous expression of two enzymes.

Published
2022
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19. Microbial production of glyceric acid, an organic acid that can be mass produced from glycerol

Author

Habe, Hiroshi, Shimada, Yuko, Yakushi, Toshiharu, Hattori, Hiromi, Ano, Yoshitaka, Fukuoka, Tokuma, Kitamoto, Dai, Itagaki, Masayuki, Watanabe, Kunihiro, Yanagishita, Hiroshi, Matsushita, Kazunobu, and Sakaki, Keiji

Subjects
Glycerin -- Usage, Glycerol -- Usage, Microbiological synthesis -- Research, Biomass energy -- Production processes, Fermentation -- Analysis, Biological sciences
Abstract

A method is developed for the efficient biotechnological production of glyceric acid (GA) as a target compound for new surplus glycerol applications in the biodiesel and oleochemical industries. The results have shown that the membrane-bound alcohol dehydrogenase (mADH) is involved in GA production by acetic acid bacteria and that GA is mass producible from glycerol feedstock by a biotechnological process.

Published
2009

20. Characterization of a cryptic, pyrroloquinoline quinone-dependent dehydrogenase of Gluconobactersp. strain CHM43

Author

Nguyen, Thuy Minh, Naoki, Kotone, Kataoka, Naoya, Matsutani, Minenosuke, Ano, Yoshitaka, Adachi, Osao, Matsushita, Kazunobu, and Yakushi, Toshiharu

Abstract

We characterized the pyrroloquinoline quinone (PQQ)-dependent dehydrogenase 9 (PQQ-DH9) of Gluconobactersp. strain CHM43, which is a homolog of PQQ-dependent glycerol dehydrogenase (GLDH). We used a plasmid construct to express PQQ-DH9. The expression host was a derivative strain of CHM43, which lacked the genes for GLDH and the membrane-bound alcohol dehydrogenase and consequently had minimal ability to oxidize primary and secondary alcohols. The membranes of the transformant exhibited considerable d-arabitol dehydrogenase activity, whereas the reference strain did not, even if it had PQQ-DH9-encoding genes in the chromosome and harbored the empty vector. This suggests that PQQ-DH9 is not expressed in the genome. The activities of the membranes containing PQQ-DH9 and GLDH suggested that similar to GLDH, PQQ-DH9 oxidized a wide variety of secondary alcohols but had higher Michaelis constants than GLDH with regard to linear substrates such as glycerol. Cyclic substrates such as cis-1,2-cyclohexanediol were readily oxidized by PQQ-DH9.Graphical AbstractPyrroloquinoline quinone-dependent dehydrogenase 9 (PQQ-DH9) of Gluconobactersp. strain CHM43 oxidizes cyclic secondary alcohols. Ox, ubiquinol oxidase; Q, ubiquinone.

Published
2021
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22. 5-keto-D-gluconate production is catalyzed by a quinoprotein glycerol dehydrogenase, major polyol dehydrogenase, in Gluconobacter species

Author

Matsushita, Kazunobu, Fujii, Yoshikazu, Ano, Yoshitaka, Toyama, Hirohide, Shinjoh, Masako, Tomiyama, Noribumi, Miyazaki, Taro, Sugisawa, Teruhide, Hoshino, Tatsuo, and Osao, Adachi

Subjects
Microbial enzymes -- Physiological aspects, Oxidation-reduction reaction -- Physiological aspects, Carbohydrate metabolism -- Physiological aspects, Oxidoreductases -- Research, Biological sciences
Abstract

Research demonstrates that the quinoproteins, D-arabitol dehydrogenase and D-sorbitol dehydrogenase are identical and catalyze D-gluconate oxidation to 5-keto-D-gluconate in Gluconobacter species. In addition, glycerol dehydrogenase has a role of a major polyol dehydrogenase mediating oxidation of sugar alcohols.

Published
2003

46. Membrane-bound Sugar Alcohol Dehydrogenase in Acetic Acid Bacteria catalyzes L-Ribulose Formation and NAD-Dependent Ribitol Dehydrogenase is Independent of the Oxidative Fermentation

Author

ADACHI, Osao, primary, FUJII, Yoshikazu, additional, ANO, Yoshitaka, additional, MOONMANGMEE, Duangtip, additional, TOYAMA, Hirohide, additional, SHINAGAWA, Emiko, additional, THEERAGOOL, Gunjana, additional, LOTONG, Napha, additional, and MATSUSHITA, Kazunobu, additional

Published
2001
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49. Conversion of Quinate to 3-Dehydroshikimate by Ca-Alginate-Immobilized Membrane of Gluconobacter oxydans IFO 3244 and Subsequent Asymmetric Reduction of 3-Dehydroshikimate to Shikimate by Immobilized Cytoplasmic NADP-Shikimate Dehydrogenase.

Author

Adachi, Osao, Ano, Yoshitaka, Shinagawa, Emiko, Yakushi, Toshiharu, and Matsushita, Kazunobu

Subjects
*ACETOBACTER, *DEHYDROGENASES, *BACTERIAL genetics, *BIOLOGICAL membranes, *PHYSISORPTION
Abstract

The article presents a study regarding the productiuon of 3-dehydroshikimate (DSA) from quinate by immobilixing the membrane fraction of the acetic acid bacteria Gluconobacter oxydans IFO 3244. The study used several methods to realize and examine the immobilization process including encapsulation, ionic binding, and physical adsorption. Results show a conversion rate of almost 100% from quinate to 3-dehydroshikimate.

Published
2010
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50. Purification and Characterization of Membrane-Bound 3-Dehydroshikimate Dehydratase from Gluconobacter oxydans IFO 3244, A New Enzyme Catalyzing Extracellular Protocatechuate Formation.

Author

Shinagawa, Emiko, Adachi, Osao, Ano, Yoshitaka, Yakushi, Toshiharu, and Matsushita, Kazunobu

Subjects
PROTEIN precursors, SOLUBILIZATION, BIOLOGICAL membranes, HOMOGENEITY, PHYSIOLOGICAL effects of enzymes
Abstract

The article presents a study that focuses on the purification and characterization of the membrane-bound 3-dehydroshikimate dehydratase (mDSD) and enzyme solubilization from the membrane fraction of gluconobacter oxydans IFO 3244. The results revealed that the mDSD in the membrane fraction suggests the mDSD's significance of aromatization, solubilized and purified to high homogeneity. It says that dehydroshikimate (DSA) was confirmed as a direct precursor of phenylcyclohexylamine (PCA).

Published
2010
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