Zobrazeno 1 - 10
of 196
pro vyhledávání: '"Tamo FUKAMIZO"'
Autor:
Takayuki Ohnuma, Jun Tsujii, Chikara Kataoka, Teruki Yoshimoto, Daijiro Takeshita, Outi Lampela, André H. Juffer, Wipa Suginta, Tamo Fukamizo
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-18 (2023)
Abstract Periplasmic solute-binding proteins (SBPs) specific for chitooligosaccharides, (GlcNAc)n (n = 2, 3, 4, 5 and 6), are involved in the uptake of chitinous nutrients and the negative control of chitin signal transduction in Vibrios. Most transl
Externí odkaz:
https://doaj.org/article/74c569eb94e74f4f9da1131c9b6c9d79
Publikováno v:
Bioresources and Bioprocessing, Vol 9, Iss 1, Pp 1-13 (2022)
Abstract Marine Vibrio species are natural degraders of chitin and usually secrete high levels of chitinolytic enzymes to digest recalcitrant chitin to chitooligosaccharides. This study used an endochitinase (VhChiA) from Vibrio campbellii to produce
Externí odkaz:
https://doaj.org/article/d09b064baf5741ad93ab4b5b4c40215f
Publikováno v:
Molecules, Vol 28, Iss 18, p 6591 (2023)
Chitooligosaccharides (COSs) are b-1,4-linked homo-oligosaccharides of N-acetylglucosamine (GlcNAc) or glucosamine (GlcN), and also include hetero-oligosaccharides composed of GlcNAc and GlcN. These sugars are of practical importance because of their
Externí odkaz:
https://doaj.org/article/3be52976fd314c2eb345a8a15257cd09
Multi-functionality of a tryptophan residue conserved in substrate-binding groove of GH19 chitinases
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-15 (2021)
Abstract GH19 and GH22 glycoside hydrolases belonging to the lysozyme superfamily have a related structure/function. A highly conserved tryptophan residue, Trp103, located in the binding groove of a GH19 chitinase from moss Bryum coronatum (BcChi-A)
Externí odkaz:
https://doaj.org/article/af857347caee45848bbbbf057bade540
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
4-O-β-tri-N-acetylchitotriosyl moranoline (GN3M) is a transition-state analogue for hen egg white lysozyme (HEWL) and identified as the most potent inhibitor till date. Isothermal titration calorimetry experiments provided the thermodynamic paramete
Externí odkaz:
https://doaj.org/article/918a08f092254b778f468a04d1607a2d
Autor:
Naoyuki Umemoto, Natsuki Saito, Masato Noguchi, Shin-ichiro Shoda, Takayuki Ohnuma, Takeshi Watanabe, Shohei Sakuda, Tamo Fukamizo
Publikováno v:
Journal of Agricultural and Food Chemistry. 70:12897-12906
Sugar oxazolines, (GlcNAc)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e51e899664bdc3f3931d6a802b42190
https://doi.org/10.1021/acs.jafc.2c04632
https://doi.org/10.1021/acs.jafc.2c04632
Publikováno v:
Journal of Agricultural and Food Chemistry. 68:5384-5390
Aspergillus niger mycelial waste is a good raw material for production of N-acetyl-d-glucosamine (GlcNAc). In this study, AnChiB, an A. niger chitinase which is upregulated during autolysis, was found to degrade A. niger mycelial waste with high effi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44790a71d3cfe00bbe92a58a22adf2ea
https://doi.org/10.1021/acs.jafc.0c01342
https://doi.org/10.1021/acs.jafc.0c01342
Publikováno v:
Plant Science. 326:111524
Two rice GH18 chitinases, Oschib1 and Oschib2, belonging to family 8 of plant pathogenesis-related proteins (PR proteins) were expressed, purified, and characterized. These enzymes, which have the structural features of class IIIb chitinases, prefere
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30de3f81e397f7f71d8206264ba719bb
https://doi.org/10.1016/j.plantsci.2022.111524
https://doi.org/10.1016/j.plantsci.2022.111524
Publikováno v:
Glycobiology. 32(4)
Plant GH19 chitinases have several loop structures, which may define their enzymatic properties. Among these loops, the longest loop, Loop-III, is most frequently conserved in GH19 enzymes. A GH19 chitinase from the moss Bryum coronatum (BcChi-A) has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2f5f07812a7298117f76f7dcf91b82f
https://pubmed.ncbi.nlm.nih.gov/34939106
https://pubmed.ncbi.nlm.nih.gov/34939106
Publikováno v:
International Journal of Biological Macromolecules. 128:985-993
Periplasmic solute-binding proteins (SBPs) serve as molecular shuttles that assist the transport of small solutes from the outer membrane to the inner membrane of all Gram-negative bacteria. Based on the available crystal structures, SBPs are classif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f16810ece350aef03dcadea60d2fdd09
https://doi.org/10.1016/j.ijbiomac.2019.02.064
https://doi.org/10.1016/j.ijbiomac.2019.02.064