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Article ; Online: Hyperinduction of pectate lyase in Dickeya chrysanthemi EC16 by plant-derived sugars

Tri Joko / Masahiro Umehara / Takeomi Murata / Hideo Etoh / Ken Izumori / Shinji Tsuyumu

Journal of Plant Interactions, Vol 13, Iss 1, Pp 141-

2018 Volume 150

Abstract: Pectate lyase (Pel) synthesis in Dickeya chrysanthemi has been reported to be hyperinduced in planta and also in the medium containing plant extract in addition to polygalacturonate. In this study, the major components of Pel-hyperinducing fractions were ...

Abstract	Pectate lyase (Pel) synthesis in Dickeya chrysanthemi has been reported to be hyperinduced in planta and also in the medium containing plant extract in addition to polygalacturonate. In this study, the major components of Pel-hyperinducing fractions were found to be glucose, fructose, and sucrose by TLC and NMR. From the analysis of the sugars and their derivatives, it was found that acyclic d-hexoses with the trans relationship between C-3 and C-5 hydroxyl groups were found to be basic structure required for hyperinducing the expression of a major isozyme in infected plants (i.e. pelE). From the fact that some non-metabolizable sugars such as 2-deoxy-d-glucose and d-fucose could lead to hyperinduction and that the hyperinduction was observed only in the medium containing low concentration (<0.25%) but not higher of the sugars was added, these sugars may be considered to participate in hyperinduction as the signal rather than through their metabolism.
Keywords	Dickeya chrysanthemi ; hyperinduction ; pectate lyase ; plant signal ; Plant culture ; SB1-1110 ; Plant ecology ; QK900-989
Subject code	580
Language	English
Publishing date	2018-01-01T00:00:00Z
Publisher	Taylor & Francis Group
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Binding of Galectin-3, a β-Galactoside-binding Lectin, to MUC1 Protein Enhances Phosphorylation of Extracellular Signal-regulated Kinase 1/2 (ERK1/2) and Akt, Promoting Tumor Cell Malignancy.

Mori, Yugo / Akita, Kaoru / Yashiro, Masakazu / Sawada, Tetsuji / Hirakawa, Kosei / Murata, Takeomi / Nakada, Hiroshi

The Journal of biological chemistry

2015 Volume 290, Issue 43, Page(s) 26125–26140

Abstract: Both mucin 1 (MUC1) and galectin-3 are known to be overexpressed in various malignant tumors and associated with a poor prognosis. It has been extensively reported that MUC1 is involved in potentiation of growth factor-dependent signal transduction. ... ...

Abstract	Both mucin 1 (MUC1) and galectin-3 are known to be overexpressed in various malignant tumors and associated with a poor prognosis. It has been extensively reported that MUC1 is involved in potentiation of growth factor-dependent signal transduction. Because some carbohydrate moieties carried on MUC1 change to preferable ones for binding of galectin-3 in cancer cells, we speculated that MUC1-mediated signaling may occur through direct binding of galectin-3. Immunochemical studies showed that the distribution of galectin-3 coincided with that of MUC1 in various human tumor tissues but not in human nonmalignant tissues, and the level of galectin-3 retained on the surface of various cancer cells paralleled that of MUC1. Treatment of MUC1-expressing cells with galectin-3 induced phosphorylation of ERK1/2 and Akt following enhanced phosphorylation of MUC1 C-terminal domain, consistently promoting tumor cell malignancy. It is also noted that this enhanced phosphorylation occurred independently of EGF receptor-mediated signaling in both EGF receptor- and MUC1-expressing cells, and multivalency of galectin-3 was important for initiation of MUC1-mediated signaling. Expectedly, both silencing of endogenous galectin-3 and treatment with galectin-3 antagonists down-regulated cell proliferation of MUC1-expressing cells. These results suggest that the binding of galectin-3 to MUC1 plays a key role in MUC1-mediated signaling. Thus, constitutive activation of MUC1-mediated signaling in an autocrine/paracrine manner caused by ligation of galectin-3 promotes uncontrolled tumor cell malignancy. This signaling may be another MUC1-mediated pathway and function in parallel with a growth factor-dependent MUC1-mediated signaling pathway.
MeSH term(s)	Cell Proliferation ; Colonic Neoplasms/enzymology ; Colonic Neoplasms/metabolism ; Colonic Neoplasms/pathology ; Galectin 3/metabolism ; HCT116 Cells ; Humans ; MAP Kinase Signaling System ; Mucin-1/metabolism ; Phosphorylation ; Protein Binding ; Proto-Oncogene Proteins c-akt/metabolism ; Signal Transduction
Chemical Substances	Galectin 3 ; MUC1 protein, human ; Mucin-1 ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1)
Language	English
Publishing date	2015-09-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M115.651489
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Article: Enzymatic synthesis of oligosaccharides and neoglycoconjugates.

Murata, Takeomi / Usui, Taichi

Bioscience, biotechnology, and biochemistry

2006 Volume 70, Issue 5, Page(s) 1049–1059

Abstract: Oligosaccharides involved in glycoconjugates play important roles in a number of biological events. To elucidate the biological functions of oligosaccharides, sufficient quantities of structurally defined oligosaccharides, are of limited availability by ... ...

Abstract	Oligosaccharides involved in glycoconjugates play important roles in a number of biological events. To elucidate the biological functions of oligosaccharides, sufficient quantities of structurally defined oligosaccharides, are of limited availability by traditional purification methods, are required. Hence, chemical and enzymatic syntheses of oligosaccharides are becoming increasingly important in glycobiology and glycotechnology. In addition, oligosaccharides often occur as glycoconjugates attached to proteins or lipids. Hence, the development of simple and effective methods for synthesizing neoglycoconjugates such as neoglycoprotein and neoglycolipids is essential for an understanding of the biological function of these molecules. Here we review the most recent developments in the enzymatic synthesis of oligosaccharides and neoglycoconjugates.
MeSH term(s)	Animals ; Carbohydrate Sequence ; Catalysis ; Glycoconjugates/biosynthesis ; Glycoside Hydrolases/chemistry ; Glycosyltransferases/chemistry ; Humans ; Molecular Sequence Data ; Mucins/biosynthesis ; Oligosaccharides/biosynthesis
Chemical Substances	Glycoconjugates ; Mucins ; Oligosaccharides ; Glycosyltransferases (EC 2.4.-) ; Glycoside Hydrolases (EC 3.2.1.-)
Language	English
Publishing date	2006-05
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1106450-x
ISSN	1347-6947 ; 0916-8451
ISSN (online)	1347-6947
ISSN	0916-8451
DOI	10.1271/bbb.70.1049
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Article: Enzymatic Synthesis of Oligosaccharides and Neoglycoconjugates

MURATA, Takeomi / USUI, Taichi

Bioscience, biotechnology, and biochemistry. 2006 May 23, v. 70, no. 5

2006

Abstract	Oligosaccharides involved in glycoconjugates play important roles in a number of biological events. To elucidate the biological functions of oligosaccharides, sufficient quantities of structurally defined oligosaccharides, are of limited availability by traditional purification methods, are required. Hence, chemical and enzymatic syntheses of oligosaccharides are becoming increasingly important in glycobiology and glycotechnology. In addition, oligosaccharides often occur as glycoconjugates attached to proteins or lipids. Hence, the development of simple and effective methods for synthesizing neoglycoconjugates such as neoglycoprotein and neoglycolipids is essential for an understanding of the biological function of these molecules. Here we review the most recent developments in the enzymatic synthesis of oligosaccharides and neoglycoconjugates.
Keywords	biotechnology ; glycoconjugates ; glycomics ; oligosaccharides
Language	English
Dates of publication	2006-0523
Size	p. 1049-1059.
Publishing place	Japan Society for Bioscience, Biotechnology, and Agrochemistry
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	1106450-x
ISSN	1347-6947 ; 0916-8451
ISSN (online)	1347-6947
ISSN	0916-8451
DOI	10.1271/bbb.70.1049
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Article ; Online: N-glycan structures of human alveoli provide insight into influenza A virus infection and pathogenesis.

Sriwilaijaroen, Nongluk / Nakakita, Shin-Ichi / Kondo, Sachiko / Yagi, Hirokazu / Kato, Koichi / Murata, Takeomi / Hiramatsu, Hiroaki / Kawahara, Toshio / Watanabe, Yohei / Kanai, Yasushi / Ono, Takao / Hirabayashi, Jun / Matsumoto, Kazuhiko / Suzuki, Yasuo

The FEBS journal

2018 Volume 285, Issue 9, Page(s) 1611–1634

Abstract: The rapidly evolvable influenza A virus has caused pandemics linked to millions of deaths in the past century. Influenza A viruses are categorized by H (hemagglutinin; HA) and N (neuraminidase; NA) proteins expressed on the viral envelope surface. ... ...

Abstract	The rapidly evolvable influenza A virus has caused pandemics linked to millions of deaths in the past century. Influenza A viruses are categorized by H (hemagglutinin; HA) and N (neuraminidase; NA) proteins expressed on the viral envelope surface. Analyses of past pandemics suggest that the HA gene segment comes from a nonhuman virus, which is then introduced into an immunologically naïve human population with potentially devastating consequences. As a prerequisite for infection, the nonhuman HA molecules of H1-H16 viruses must be able to bind to specific sialyl receptors on the host cell surface along the human respiratory tract. Thus, additional insight into the structures of host cell glycans and how different HAs interact with different glycans might provide new insight into the mechanisms underlying sustained infection and transmission in humans. In this work, we identified the sialyl N-glycans found in normal human alveoli and characterized the influenza viruses that preferentially bound to these different structures. We also determined the amino acid changes in HA that were linked to a switch of receptor-binding preference from nonhuman to pandemic, as well as pandemic to seasonal. Our data provide insight into why seasonal viruses are associated with reduced alveolar infection and damage and suggest new considerations for designing anti-HA vaccines and drugs. The results provide a better understanding of viral tropism and pathogenesis in humans that will be important for prediction and surveillance of zoonotic, pandemic, and epidemic influenza outbreaks. Database: The novel hemagglutinin nucleotide sequences reported here were deposited in GISAID under the accession numbers of EPI685738 for A/Yamaguchi/20/2006(H1N1) and EPI685740 for A/Kitakyushu/10/2006(H1N1).
MeSH term(s)	Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Binding, Competitive ; Carbohydrate Sequence ; Disease Outbreaks ; Dogs ; Ducks ; Hemagglutinin Glycoproteins, Influenza Virus/chemistry ; Hemagglutinin Glycoproteins, Influenza Virus/genetics ; Humans ; Influenza A virus/chemistry ; Influenza A virus/genetics ; Influenza A virus/physiology ; Influenza in Birds/epidemiology ; Influenza in Birds/pathology ; Influenza in Birds/virology ; Influenza, Human/epidemiology ; Influenza, Human/pathology ; Influenza, Human/virology ; Madin Darby Canine Kidney Cells ; Orthomyxoviridae Infections/epidemiology ; Orthomyxoviridae Infections/pathology ; Orthomyxoviridae Infections/virology ; Pandemics ; Polysaccharides/chemistry ; Polysaccharides/physiology ; Poultry Diseases/epidemiology ; Poultry Diseases/pathology ; Poultry Diseases/virology ; Protein Binding ; Pulmonary Alveoli/chemistry ; Pulmonary Alveoli/pathology ; Pulmonary Alveoli/virology ; RNA, Viral/genetics ; Receptors, Virus/chemistry ; Seasons ; Sialic Acids/chemistry ; Swine ; Swine Diseases/epidemiology ; Swine Diseases/pathology ; Swine Diseases/virology ; Viral Tropism/physiology ; Virus Replication ; Zoonoses
Chemical Substances	Hemagglutinin Glycoproteins, Influenza Virus ; Polysaccharides ; RNA, Viral ; Receptors, Virus ; Sialic Acids ; hemagglutinin, human influenza A virus
Language	English
Publishing date	2018-04-11
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.14431
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Article ; Online: Enzymatic synthesis of gentiooligosaccharides by transglycosylation with beta-glycosidases from Penicillium multicolor.

Fujimoto, Yoshinori / Hattori, Takeshi / Uno, Shuji / Murata, Takeomi / Usui, Taichi

Carbohydrate research

2009 Volume 344, Issue 8, Page(s) 972–978

Abstract: A crude enzyme preparation from Penicillium multicolor efficiently produced mainly gentiotriose to gentiopentaose (d.p. 3-5) by transglycosylation using a high concentration of gentiobiose as the substrate. The resulting gentiotriose was examined in a ... ...

Abstract	A crude enzyme preparation from Penicillium multicolor efficiently produced mainly gentiotriose to gentiopentaose (d.p. 3-5) by transglycosylation using a high concentration of gentiobiose as the substrate. The resulting gentiotriose was examined in a gustatory sensation test using human volunteers, and was determined to have one-fifth of the bitterness of gentiobiose. The crude enzyme preparation was analyzed by chromatography to determine the enzyme responsible for formation of the gentiooligosaccharides. The transglycosylation was shown to take place in two stages by a combination of beta-glucosidase and beta-(1-->6)-glucanase. In the initial stage, which was the rate-limiting step in the overall process, beta-glucosidase produced mainly gentiotriose from gentiobiose. In the second step, beta-(1-->6)-glucanase acted on the resulting gentiotriose, which served as both donor and acceptor, to produce a series of gentiooligosaccharides (d.p. 4-9) by transglycosylation.
MeSH term(s)	Carbohydrate Sequence ; Chromatography, High Pressure Liquid ; Glycosylation ; Molecular Sequence Data ; Molecular Structure ; Oligosaccharides/chemical synthesis ; Oligosaccharides/chemistry ; Penicillium/enzymology ; beta-Glucosidase/metabolism
Chemical Substances	Oligosaccharides ; beta-Glucosidase (EC 3.2.1.21)
Language	English
Publishing date	2009-05-26
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1435-7
ISSN	1873-426X ; 0008-6215
ISSN (online)	1873-426X
ISSN	0008-6215
DOI	10.1016/j.carres.2009.03.006
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Article: N‐glycan structures of human alveoli provide insight into influenza A virus infection and pathogenesis

Sriwilaijaroen, Nongluk / Hiroaki Hiramatsu / Hirokazu Yagi / Jun Hirabayashi / Kazuhiko Matsumoto / Koichi Kato / Sachiko Kondo / Shin‐ichi Nakakita / Takao Ono / Takeomi Murata / Toshio Kawahara / Yasuo Suzuki / Yasushi Kanai / Yohei Watanabe

FEBS journal. 2018 May, v. 285, no. 9

2018

Abstract	The rapidly evolvable influenza A virus has caused pandemics linked to millions of deaths in the past century. Influenza A viruses are categorized by H (hemagglutinin; HA) and N (neuraminidase; NA) proteins expressed on the viral envelope surface. Analyses of past pandemics suggest that the HA gene segment comes from a nonhuman virus, which is then introduced into an immunologically naïve human population with potentially devastating consequences. As a prerequisite for infection, the nonhuman HA molecules of H1–H16 viruses must be able to bind to specific sialyl receptors on the host cell surface along the human respiratory tract. Thus, additional insight into the structures of host cell glycans and how different HAs interact with different glycans might provide new insight into the mechanisms underlying sustained infection and transmission in humans. In this work, we identified the sialyl N‐glycans found in normal human alveoli and characterized the influenza viruses that preferentially bound to these different structures. We also determined the amino acid changes in HA that were linked to a switch of receptor‐binding preference from nonhuman to pandemic, as well as pandemic to seasonal. Our data provide insight into why seasonal viruses are associated with reduced alveolar infection and damage and suggest new considerations for designing anti‐HA vaccines and drugs. The results provide a better understanding of viral tropism and pathogenesis in humans that will be important for prediction and surveillance of zoonotic, pandemic, and epidemic influenza outbreaks. DATABASE: The novel hemagglutinin nucleotide sequences reported here were deposited in GISAID under the accession numbers of EPI685738 for A/Yamaguchi/20/2006(H1N1) and EPI685740 for A/Kitakyushu/10/2006(H1N1).
Keywords	amino acids ; genes ; hemagglutinins ; human population ; humans ; influenza ; Influenza A virus ; monitoring ; nucleotide sequences ; pandemic ; pathogenesis ; polysaccharides ; prediction ; receptors ; respiratory system ; sialidase ; vaccines ; viruses
Language	English
Dates of publication	2018-05
Size	p. 1611-1634.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	JOURNAL ARTICLE
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.14431
Database	NAL-Catalogue (AGRICOLA)

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Article: Enzymatic synthesis of spacer-linked divalent glycosides carrying N-acetylglucosamine and N-acetyllactosamine: analysis of cross-linking activities with WGA.

Misawa, Yoshinori / Akimoto, Takashi / Amarume, Satoshi / Murata, Takeomi / Usui, Taichi

Journal of biochemistry

2008 Volume 143, Issue 1, Page(s) 21–30

Abstract: Divalent glycosides carrying N-acetyl-d-glucosamine (GlcNAc) and N-acetyllactosamine (LacNAc) were designed and prepared as glycomimetics. First, hexan-1,6-diyl bis-(2-acetamido-2-deoxy-beta-d-glucopyranoside) (GlcNAc-Hx-GlcNAc) and 3,6-dioxaoct-1,8-diyl ...

Abstract	Divalent glycosides carrying N-acetyl-d-glucosamine (GlcNAc) and N-acetyllactosamine (LacNAc) were designed and prepared as glycomimetics. First, hexan-1,6-diyl bis-(2-acetamido-2-deoxy-beta-d-glucopyranoside) (GlcNAc-Hx-GlcNAc) and 3,6-dioxaoct-1,8-diyl bis-(2-acetamido-2-deoxy-beta-d-glucopyranoside) (GlcNAc-Doo-GlcNAc) were enzymatically synthesized by transglycosylation of an N,N'N'',N'''-tetraacetylchitotetraose [(GlcNAc)(4)] donor with a primary diol acceptor, utilizing a chitinolytic enzyme from Amycolatopsis orientalis. The resulting divalent glycosides were further converted to the respective hexan-1,6-diyl bis-[beta-d-galactopyranosyl-(1-->4)-2-acetamido-2-deoxy-beta-d-glucopyranoside] (LacNAc-Hx-LacNAc) and 6-(2-acetamido-2-deoxy-beta-d-glucopyranosyl)-hexyl beta-d-galactopyranosyl-(1-->4)-2-acetamido-2-deoxy-beta-d-glucopyranoside (LacNAc-Hx-GlcNAc), and respective 3,6-dioxaoct-1,8-diyl bis-[beta-d-galactopyranosyl-(1-->4)-2-acetamido-2-deoxy-beta-d-glucopyranoside] (LacNAc-Doo-LacNAc) and 8-(2-acetamido-2-deoxy-beta-d-glucopyranosyl)-3,6-dioxaoctyl beta-d-galactopyranosyl-(1-->4)-2-acetamido-2-deoxy-beta-d-glucopyranoside (LacNAc-Doo-GlcNAc) by galactosyltransferase. The interaction of wheat germ agglutinin (WGA) with a series of divalent glycosides and related compounds were studied using a biosensor based on surface plasmon resonance (SPR) and by precipitation analysis. Our results demonstrated that divalent glycosides carrying GlcNAc on both sides and GlcNAc and LacNAc on each side are capable of precipitating WGA as divalent ligands, but that the corresponding monovalent controls and divalent glycosides carrying LacNAc on both sides are unable to precipitate the lectin and bind as univalent ligands.
MeSH term(s)	Acetylglucosamine/chemistry ; Actinomycetales/enzymology ; Amino Sugars/chemistry ; Chemical Precipitation ; Cross-Linking Reagents/chemistry ; Cross-Linking Reagents/metabolism ; Galactosyltransferases/metabolism ; Glycosides/biosynthesis ; Glycosides/chemistry ; Glycosides/metabolism ; Hemagglutination Inhibition Tests ; Ligands ; Surface Plasmon Resonance ; Wheat Germ Agglutinins/metabolism
Chemical Substances	Amino Sugars ; Cross-Linking Reagents ; Glycosides ; Ligands ; Wheat Germ Agglutinins ; N-acetyllactosamine (3Y5B2K5OOK) ; Galactosyltransferases (EC 2.4.1.-) ; Acetylglucosamine (V956696549)
Language	English
Publishing date	2008-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218073-x
ISSN	1756-2651 ; 0021-924X
ISSN (online)	1756-2651
ISSN	0021-924X
DOI	10.1093/jb/mvm200
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Article: Enzymatic synthesis of poly-N-acetyllactosamines as potential substrates for endo-beta-galactosidase-catalyzed hydrolytic and transglycosylation reactions.

Murata, Takeomi / Honda, Hiroki / Hattori, Takeshi / Usui, Taichi

Biochimica et biophysica acta

2005 Volume 1722, Issue 1, Page(s) 60–68

Abstract: Enzymatic synthesis of GlcNAc-terminated poly-N-acetyllactosamine beta-glycosides GlcNAcbeta1,3(Galbeta1,4GlcNAcbeta1,3)(n)Galbeta1,4GlcNAcbeta-pNP (n=1-4) was demonstrated using a transglycosylation reaction of Escherichia freundii endo-beta- ... ...

Abstract	Enzymatic synthesis of GlcNAc-terminated poly-N-acetyllactosamine beta-glycosides GlcNAcbeta1,3(Galbeta1,4GlcNAcbeta1,3)(n)Galbeta1,4GlcNAcbeta-pNP (n=1-4) was demonstrated using a transglycosylation reaction of Escherichia freundii endo-beta-galactosidase. The enzyme catalyzed a transglycosylation reaction on GlcNAcbeta1,3Galbeta1,4GlcNAcbeta-pNP (1), which served both as a donor and an acceptor, and converted 1 into p-nitrophenyl beta-glycosides GlcNAcbeta1,3(Galbeta1,4GlcNAcbeta1,3)(1)Galbeta1,4GlcNAcbeta-pNP (2), GlcNAcbeta1,3(Galbeta1,4GlcNAcbeta1,3)(2)Galbeta1,4GlcNAcbeta-pNP (3), GlcNAcbeta1,3(Galbeta1,4GlcNAcbeta1,3)(3)Galbeta1,4GlcNAcbeta-pNP (4) and GlcNAcbeta1,3(Galbeta1,4GlcNAcbeta1,3)(4)Galbeta1,4GlcNAcbeta-pNP (5). When 2 was used as an initial substrate, it led to the preferential synthesis of nonasaccharide beta-glycoside 4 to heptasaccharide beta-glycoside 3. This suggests that 4 is directly synthesized by transferring the tetrasaccharide unit GlcNAcbeta1,3Galbeta1,4GlcNAcbeta1,3Gal to nonreducing end GlcNAc residue of 2 itself. The efficiency of production of poly-N-acetyllactosamines by E. freundii endo-beta-galactosidase was significantly enhanced by the addition of BSA and by a low-temperature condition. Resulting 2 and 3 were shown to be useful for studying endo-beta-galactosidase-catalyzed hydrolytic and transglycosylation reactions.
MeSH term(s)	Animals ; Bacterial Proteins/metabolism ; Carbohydrate Sequence ; Glycoside Hydrolases/metabolism ; Glycosylation ; Molecular Sequence Data ; Polysaccharides/chemical synthesis ; Polysaccharides/chemistry ; Polysaccharides/metabolism
Chemical Substances	Bacterial Proteins ; Polysaccharides ; poly-N-acetyllactosamine (82441-98-3) ; Glycoside Hydrolases (EC 3.2.1.-) ; keratan-sulfate endo-1,4-beta-galactosidase (EC 3.2.1.103)
Language	English
Publishing date	2005-02-11
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagen.2004.11.008
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Article ; Online: Molecular design of fluorescent labeled glycosides as acceptor substrates for sialyltransferases.

Ogata, Makoto / Obara, Takakiyo / Chuma, Yasushi / Murata, Takeomi / Park, Enoch Y / Usui, Taichi

Bioscience, biotechnology, and biochemistry

2010 Volume 74, Issue 11, Page(s) 2287–2292

Abstract: A series of dansyl-labeled glycosides with di-, tetra-, and hexasaccharides carrying the terminal N-acetyllactosamine (LacNAc) sequence were synthesized as acceptor substrates for α2,6- and α2,3-sialyltransferases. As an alternative design, dansyl- ... ...

Abstract	A series of dansyl-labeled glycosides with di-, tetra-, and hexasaccharides carrying the terminal N-acetyllactosamine (LacNAc) sequence were synthesized as acceptor substrates for α2,6- and α2,3-sialyltransferases. As an alternative design, dansyl-labeled LacNAc glycoside carrying a long-spacer linked glycan was engineered by replacement of the LacNAc or lactose units with an alkyl chain. In addition, we designed a dansyl-labeled bi-antennary LacNAc glycoside as an N-linked oligosaccharide mimetic, such as asialo-α(1)-acid glycoprotein. The kinetic parameters for the transfer reaction of synthesized dansyl-labeled glycosides by sialyltransferases were determined by the fluorescent HPLC method. The catalytic efficiencies (V(max)/K(m)) of acceptor substrates carrying the terminal LacNAc sequence with various length glycans in the array for α2,6- and α2,3-sialyltransferases decreased in a glycan length-dependent manner. Furthermore, of the acceptor substrates tested, dansyl-labeled bi-antennary LacNAc glycoside displayed the most favorable K(m) value for α2,6- and α2,3-sialyltransferases.
MeSH term(s)	Amino Sugars ; Dansyl Compounds ; Fluorescent Dyes/chemistry ; Glycosides/chemistry ; Glycosides/metabolism ; Kinetics ; Oligosaccharides ; Protein Binding ; Sialyltransferases/metabolism
Chemical Substances	Amino Sugars ; Dansyl Compounds ; Fluorescent Dyes ; Glycosides ; Oligosaccharides ; N-acetyllactosamine (3Y5B2K5OOK) ; Sialyltransferases (EC 2.4.99.-)
Language	English
Publishing date	2010
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1106450-x
ISSN	1347-6947 ; 0916-8451
ISSN (online)	1347-6947
ISSN	0916-8451
DOI	10.1271/bbb.100505
Database	MEDical Literature Analysis and Retrieval System OnLINE

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