Struktura a mechanismus glykosyltransferas

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F06%3A00015567" target="_blank" >RIV/00216224:14310/06:00015567 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Structures and mechanisms of glycosyltransferases

Popis výsledku v původním jazyce

Glycosyltransferases catalyze the transfer of a sugar moiety from an activated donor sugar onto saccharide and non-saccharide acceptors. A sequence-based classification spreads glycosyltransferases in a large number of families thus reflecting the variety of molecules that can be used as acceptors. In contrast, this enzyme family is characterized by a more conserved 3D architecture. Until recently, only two different folds (GT-A and GT-B) have been identified for solved crystal structures. The recent report of a structure for a bacterial sialyltransferase allows the defination of a new fold family. Progress in the elucidation of the structures and mechanisms of glycosyltransferases are discussed in this review. To accomodate the growing number of crystal structures, the 3D-glycosyltransferase database has been created to gather structural information concerning this class of enzymes.

Název v anglickém jazyce

Structures and mechanisms of glycosyltransferases

Popis výsledku anglicky

Glycosyltransferases catalyze the transfer of a sugar moiety from an activated donor sugar onto saccharide and non-saccharide acceptors. A sequence-based classification spreads glycosyltransferases in a large number of families thus reflecting the variety of molecules that can be used as acceptors. In contrast, this enzyme family is characterized by a more conserved 3D architecture. Until recently, only two different folds (GT-A and GT-B) have been identified for solved crystal structures. The recent report of a structure for a bacterial sialyltransferase allows the defination of a new fold family. Progress in the elucidation of the structures and mechanisms of glycosyltransferases are discussed in this review. To accomodate the growing number of crystal structures, the 3D-glycosyltransferase database has been created to gather structural information concerning this class of enzymes.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GD204%2F03%2FH016" target="_blank" >GD204/03/H016: Strukturní biofyzika makromolekul</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2006

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Glycobiology

ISSN

0959-6658

e-ISSN

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Svazek periodika

16

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

9

Strana od-do

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Kód UT WoS článku

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EID výsledku v databázi Scopus

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