Informacja

Drogi użytkowniku, aplikacja do prawidłowego działania wymaga obsługi JavaScript. Proszę włącz obsługę JavaScript w Twojej przeglądarce.

Wyszukujesz frazę "glycosyltransferase" wg kryterium: Temat


Wyświetlanie 1-3 z 3
Tytuł:
High-resolution structure of NodZ fucosyltransferase involved in the biosynthesis of the nodulation factor
Autorzy:
Brzezinski, Krzysztof
Stepkowski, Tomasz
Panjikar, Santosh
Bujacz, Grzegorz
Jaskolski, Mariusz
Powiązania:
https://bibliotekanauki.pl/articles/1040936.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
nitrogen fixation
glycosyltransferase
nodulation
NodZ
fucosyltransferase
Opis:
The fucosyltransferase NodZ is involved in the biosynthesis of the nodulation factor in nitrogen-fixing symbiotic bacteria. It catalyzes α1,6 transfer of l-fucose from GDP-fucose to the reducing residue of the synthesized Nod oligosaccharide. We present the structure of the NodZ protein from Bradyrhizobium expressed in Escherichia coli and crystallized in the presence of phosphate ions in two crystal forms. The enzyme is arranged into two domains of nearly equal size. Although NodZ falls in one broad class (GT-B) with other two-domain glycosyltransferases, the topology of its domains deviates from the canonical Rossmann fold, with particularly high distortions in the N-terminal domain. Mutational data combined with structural and sequence alignments indicate residues of potential importance in GDP-fucose binding or in the catalytic mechanism. They are all clustered in three conserved sequence motifs located in the C-terminal domain.
Źródło:
Acta Biochimica Polonica; 2007, 54, 3; 537-549
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Mechanistic variation in the glycosyltransfer of N-acetylneuraminic acid
Autorzy:
Horenstein, B.
Yang, J.
Bruner, M.
Powiązania:
https://bibliotekanauki.pl/articles/146968.pdf
Data publikacji:
2002
Wydawca:
Instytut Chemii i Techniki Jądrowej
Tematy:
CMP-NeuAc
glycosyltransferase
isotope effects
kinetics
sialyltransferase
trans-sialidase
transition state
Opis:
N-acetylneuraminic acid is an acidic nine-carbon amino ketose typically found at the non-reducing terminus of glycoproteins and glycolipids. The presence of a carboxylate group adjacent to the anomeric center suggest that this sugar could have transition states with highly stabilized oxocarbenium ion character during transfer reactions at the anomeric carbon. Kinetic isotope effect (KIE) experiments were used to probe the transition state for solvolysis of UMP-NeuAc, sialyltransferase-catalyzed transfer of UMP-NeuAc to N-acetyl-lactosamine, trans-sialidase catalyzed transfer of alfa(2--3) Neu-Lac or alfa(2--3) Neu-Gal, and acid catalyzed hydrolysis of alfa(2--3) Neu-Lac. The two key positions of isotope substitution in the N-acetyl neuraminic acid residue were the C3’ position, di-substituted with deuterium, and the C2’ position, substituted with either carbon-13 or carbon-14. The solvolysis reaction had a beta–2H KIE of 1.28 and a primary 14C KIE of 1.03. The sialyltransferase-catalyzed reaction had a b-2H KIE of 1.22 and a 14C KIE of 1.03. Trans-sialidase had a b–2H KIE of 1.05 and a primary 13C KIE of 1.03, equivalent to a 14C KIE of 1.06. Solvolysis of the trans-sialidase substrate gave a beta-2H KIE of 1.06, and a primary 13C KIE of 1.015. The results indicate a very late transition state for solvolysis of CMP-NeuAc, without nucleophilic participation. The sialyltransferase transition state is similar, but with less charge development. Trans-sialidase has a transition state with diminished charge development and considerable nucleophilic character, which leads to a covalent intermediate. The glycosyltransfer of N-acetylneuraminic acid glycosides is not limited to the classical dissociative mechanism.
Źródło:
Nukleonika; 2002, 47,suppl.1; 25-28
0029-5922
1508-5791
Pojawia się w:
Nukleonika
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Expression of UDP-dependent glycosyltransferase genes in correlation to steviol glycosides presence in Stevia rebaudiana
Autorzy:
Libik-Konieczny, M.
Michalec, Z.
Rozpadek, P.
Dziurka, M.
Capecka, E.
Matkowski, A.
Miszalski, Z.
Powiązania:
https://bibliotekanauki.pl/articles/80470.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
conference
Stevia rebaudiana
diterpene glycoside
sweetener
food product
steviol glycoside
gene expression
UDP-dependent glycosyltransferase
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 2
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

    Ta witryna wykorzystuje pliki cookies do przechowywania informacji na Twoim komputerze. Pliki cookies stosujemy w celu świadczenia usług na najwyższym poziomie, w tym w sposób dostosowany do indywidualnych potrzeb. Korzystanie z witryny bez zmiany ustawień dotyczących cookies oznacza, że będą one zamieszczane w Twoim komputerze. W każdym momencie możesz dokonać zmiany ustawień dotyczących cookies