X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family

Autor:	Uitdehaag, JCM, Mosi, R, Kalk, KH, Dijkhuizen, L, Withers, SG, Dijkstra, BW
Přispěvatelé:	Groningen Biomolecular Sciences and Biotechnology
Jazyk:	angličtina
Rok vydání:	1999
Předmět:	MECHANISM RESOLUTION GLUCOSIDASE PRODUCT SPECIFICITY MAPS ERRORS DIFFRACTION PROTEIN STRUCTURES HYDROLYSIS COEFFICIENTS
Zdroj:	Nature Structural Biology, 6(5), 432-436
ISSN:	1072-8368
Popis:	Cyclodextrin glycosyltransferase (CGTase) is an enzyme of the alpha-amylase family, which uses a double displacement mechanism to process alpha-linked glucose polymers. We have determined two X-ray structures of CGTase complexes, one with an intact substrate at 2.1 Angstrom resolution, and the other with a covalently bound reaction Intermediate at 1.8 Angstrom resolution. These structures give evidence for substrate distortion and the covalent character of the intermediate and for the first time show, in atomic detail, how catalysis in the alpha-amylase family proceeds by the concerted action of all active site residues.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=narcis______::d41a5c7084fabf78d710ff67e0b2f689 https://research.rug.nl/en/publications/f95e3cae-fdaf-4322-b355-8eaf1e075070 Zobrazit plný text záznamu Full text from SpringerLink