Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Tomoki Hamamoto"'
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 69:1944-1950
We have established an efficient method for enzymatic production of cytidine 5'-monophospho-N-acetylneuraminic acid (CMP-NeuAc) from inexpensive materials, N-acetylglucosamine (GlcNAc) and cytidine 5'-monophosphate (CMP). The Haemophilus influenzae n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c243b954c938047aef8392a6939da4f3
https://doi.org/10.1271/bbb.69.1944
https://doi.org/10.1271/bbb.69.1944
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 67:989-995
Nucleoside deoxyribosyltransferase-II (NdRT-II) of Lactobacillus helveticus, which catalyzes the transfer of a glycosyl residue from a donor deoxyribonucleoside to an acceptor base, has a broad specificity for the acceptor bases. Six-substituted puri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a614dbba6509049671ebf15e30ddd77
https://doi.org/10.1271/bbb.67.989
https://doi.org/10.1271/bbb.67.989
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 65:1736-1740
A novel method for synthesizing CMP-NeuAc was established. We first confirmed that the putative neuA gene of Haemophilus influenzae, identified by its whole genome sequence project, indeed encodes CMP-NeuAc synthetase (EC 2.7.7.43). The enzyme requir
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fd1a157b7fcfd8b235473eaaea08daa
https://doi.org/10.1271/bbb.65.1736
https://doi.org/10.1271/bbb.65.1736
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 64:386-392
Uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc) has been synthesized by a yeast-based method from 5'-UMP and glucosamine, in which yeast cells catalyze the conversion of 5'-UMP to 5'-UTP and provide enzymes involved in UDP-GlcNAc synthesis usin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7babdba381a1f2eb7badcc215a3af9a8
https://doi.org/10.1271/bbb.64.386
https://doi.org/10.1271/bbb.64.386
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 62:1103-1108
Phosphopentomutase catalyzes the transfer of an intramolecular phosphate on ribose or deoxyribose, and is involved in the salvage pathway of nucleoside synthesis. We identified a sequence 5'-upstream of the genes for the nucleoside phosphorylases of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c54f482b1e08357de1c398287a44a577
https://doi.org/10.1271/bbb.62.1103
https://doi.org/10.1271/bbb.62.1103
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 61:276-280
Bacillus stearothermophilus TH 6-2 has two kinds of purine nucleoside phosphorylases (Pu-NPases). The type I enzyme (Pu-NPase I) is a functional and structural homolog of eukaryotic purine nucleoside phosphorylases that catalyze the phosphorolysis of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5adf74e96fe8597c977c0ec977ac6061
https://doi.org/10.1271/bbb.61.276
https://doi.org/10.1271/bbb.61.276
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 60:1655-1659
The pyrimidine nucleoside phosphorylase (Py-NPase) of Bacillus stearothermophilus TH 6-2 is a dimer of 46-kDa subunits and catalyzes the reversible phosphorolysis of uridine and thymidine. The gene encoding this pyrimidine nucleoside phosphorylase (p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfab4c1c71b3708e847056a5324f4acf
https://doi.org/10.1271/bbb.60.1655
https://doi.org/10.1271/bbb.60.1655
Autor:
Naoki Fujitani, Takahiko Matsushita, Kentarou Naruchi, Shin-Ichiro Nishimura, Hirosato Kondo, Tomoki Hamamoto, Hiroshi Hinou, Masaki Kurogochi, Hiroki Shimizu
Publikováno v:
ChemInform. 38
We have established a facile and efficient protocol for the preparative-scale synthesis of various compound libraries related to lactosaminoglycans: cell surface oligosaccharides composed of N-acetyllactosamine as a repeating disaccharide unit, based
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4d1ab01ff2dee03dddc6f8395f23441
https://doi.org/10.1002/chin.200714203
https://doi.org/10.1002/chin.200714203
Publikováno v:
Bioscience, biotechnology, and biochemistry. 61(2)
Bacillus stearothermophilus TH 6-2 has two kinds of purine nucleoside phosphorylases (Pu-NPase I and Pu-NPase II). The Pu-NPase I is a functional homolog of eukaryotic purine nucleoside phosphorylases that can catalyze the phosphorolysis of inosine a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3530c02d9a9074c4d67d2a81ff9eef08
https://pubmed.ncbi.nlm.nih.gov/9058965
https://pubmed.ncbi.nlm.nih.gov/9058965
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 60:1179-1180
The purine nucleoside phosphorylase (Pu-NPase) and the pyrimidine nucleoside phosphorylase (Py-NPase) have been purified from Bacillus stearothermophilus TH 6-2. The Pu-NPase is a trimer of 30-kDa subunits and the Py-NPase is a dimer of 46-kDa subuni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f98b245a426a7ada6debb68a1f7c4e5
https://doi.org/10.1271/bbb.60.1179
https://doi.org/10.1271/bbb.60.1179