Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Takenori Satomura"'
Autor:
Miku Maeno, Taketo Ohmori, Daiki Nukada, Haruhiko Sakuraba, Takenori Satomura, Toshihisa Ohshima
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1871:140904
Autor:
Toshihisa Ohshima, Takenori Satomura, Junji Hayashi, Shin-ichiro Suye, Haruhiko Sakuraba, Tatsuya Ohshida
Publikováno v:
Extremophiles. 22:975-981
A gene-encoding a dye-linked D-lactate dehydrogenase (Dye-DLDH) homolog was identified in the genome of the hyperthermophilic archaeon Thermoproteus tenax. The gene was expressed in Escherichia coli and the product was purified to homogeneity. The re
Autor:
Shin-ichiro Suye, Shunsuke Taki, Eiichiro Takamura, Haruhiko Sakuraba, Takenori Satomura, Toshihisa Ohshima, Hiroaki Sakamoto
Publikováno v:
Applied biochemistry and biotechnology. 193(2)
Enzymes from hyperthermophilic archaea are potential candidates for industrial use because of their superior pH, thermal, and long-term stability, and are expected to improve the long-term stability of biofuel cells (BFCs). However, the reported mult
Autor:
Toshihisa Ohshima, Shin-ichiro Suye, Norio Kurosawa, Takenori Satomura, Haruhiko Sakuraba, Shin Emoto
Publikováno v:
Journal of bioscience and bioengineering. 130(3)
A gene encoding a dye-linked d -amino acid dehydrogenase (Dye-DADH) homologue was found in a hyperthermophilic archaeon, Sulfurisphaera tokodaii. The predicted amino acid sequence suggested that the gene product is a membrane-bound type enzyme. The g
Autor:
Haruhiko Sakuraba, Tatsuya Ohshida, Takenori Satomura, Ryushi Kawakami, Toshihisa Ohshima, Junji Hayashi
Publikováno v:
Protein Expression and Purification. 126:62-68
2-Deoxy-d-ribose-5-phosphate aldolase (DERA) catalyzes the aldol reaction between two aldehydes and is thought to be a potential biocatalyst for the production of a variety of stereo-specific materials. A gene encoding DERA from the extreme halophili
Publikováno v:
Applied Microbiology and Biotechnology. 99:9337-9347
Dye-linked D-amino acid dehydrogenases (Dye-DADHs) catalyze the dehydrogenation of free D-amino acids in the presence of an artificial electron acceptor. Although Dye-DADHs functioning in catabolism of L-alanine and as primary enzymes in electron tra
Publikováno v:
Journal of Bacteriology. 196:3793-3806
The Bacillus subtilis ilv-leu operon functions in the biosynthesis of branched-chain amino acids. It undergoes catabolite activation involving a promoter-proximal cre which is mediated by the complex of CcpA and P-Ser-HPr. This activation of ilv-leu
Autor:
Gaku Koizumi, Shin-ichiro Suye, Hiroaki Sakamoto, Ayako Koto, Kazuya Watanabe, Takenori Satomura, Seiya Watanabe
Publikováno v:
Sensing and Bio-Sensing Research, Vol 4, Iss C, Pp 37-39 (2015)
l -hydroxyproline ( l -Hyp: trans -4-hydroxy- l -proline) is commonly found at high concentrations in connective tissue proteins such as collagen. It is a remarkably useful molecular marker because variation in the level of l -Hyp is associated with
The Bacillus subtilis rhaEWRBMA (formerly yuxG-yulBCDE ) operon consists of four genes encoding enzymes for l -rhamnose catabolism and the rhaR gene encoding a DeoR-type transcriptional regulator. DNase I footprinting analysis showed that the RhaR pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::047f5ac35ae235c4fe5aa01d293ee8a1
https://europepmc.org/articles/PMC4810612/
https://europepmc.org/articles/PMC4810612/
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65:199-203
The crystal structure of a D-tagatose 3-epimerase-related protein (TM0416p) encoded by the hypothetical open reading frame TM0416 in the genome of the hyperthermophilic bacterium Thermotoga maritima was determined at a resolution of 2.2 A. The asymme