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Article

Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase.

European journal of biochemistry - 1 Jan 2004

Synstad Bjørnar, Gåseidnes Sigrid, Van Aalten Daan M F, Vriend Gert, Nielsen Jens E, Eijsink Vincent G H

Abstract excerpt

Glycoside hydrolysis by retaining family 18 chitinases involves a catalytic acid (Glu) which is part of a conserved DXDXE sequence motif that spans strand four of a (betaalpha)8 barrel (TIM barrel) structure. These glycoside hydrolases are unusual in that the positive charge emerging on the anomeric carbon after departure of the leaving group is stabilized by the substrate itself (the N-acetyl group of the...

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Source

Identifiers

PMID: 14717693
DOI: 10.1046/j.1432-1033.2003.03923.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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