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. 1999 May;6(5):432-6.
doi: 10.1038/8235.

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

J C Uitdehaag  1 , R Mosi, K H Kalk, B A van der Veen, L Dijkhuizen, S G Withers, B W Dijkstra
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X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family

J C Uitdehaag et al. Nat Struct Biol. 1999 May.

Abstract

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 A resolution, and the other with a covalently bound reaction intermediate at 1.8 A 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.

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Comment in

  • Trapped in the act of catalysis.
    Davies GJ, Wilson KS. Davies GJ, et al. Nat Struct Biol. 1999 May;6(5):406-8. doi: 10.1038/8200. Nat Struct Biol. 1999. PMID: 10331861 No abstract available.

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