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Bacterial 1,3-1,4-beta-glucanases: structure, function and protein engineering.

A Planas
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Abstract

1,3-1,4-beta-Glucanases (or lichenases, EC 3.2.1.73) hydrolyse linear beta-glucans containing beta-1,3 and beta-1,4 linkages such as cereal beta-glucans and lichenan, with a strict cleavage specificity for beta-1,4 glycosidic bonds on 3-O-substituted glucosyl residues. The bacterial enzymes are retaining glycosyl hydrolases of family 16 with a jellyroll beta-sandwich fold and a substrate binding cleft composed of six subsites. The present paper reviews the structure-function aspects of the enzymatic action including mechanistic enzymology, protein engineering and X-ray crystallographic studies.

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Amino Acid SequenceBacillusBacteriaBinding SitesCarbohydrate SequenceGenes, BacterialGlucansGlycoside HydrolasesGlycosyltransferasesKineticsModels, MolecularMolecular Sequence DataMutationProtein ConformationProtein EngineeringSequence AlignmentStructure-Activity RelationshipSubstrate SpecificityJournal ArticleResearch Support, Non-U.S. Gov'tReview

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A Planas. 2000-12-29. Bacterial 1,3-1,4-beta-glucanases: structure, function and protein engineering.. https://doi.org/10.1016/s0167-4838(00)00231-4

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