Bacterial 1,3-1,4-beta-glucanases: structure, function and protein engineering.
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.
Planas
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Laboratory of Biochemistry, Institut Químic de Sarrià, Universitat Ramon Llull, Via Augusta, 390, 08017, Barcelona, Spain. aplan@iqus.es
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology; D001419:Bacteria / Q000201:enzymology* / Q000235:genetics; D001665:Binding Sites; D002240:Carbohydrate Sequence; D005798:Genes, Bacterial; D005936:Glucans / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000378:metabolism; D016695:Glycosyltransferases / Q000737:chemistry; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D015202:Protein Engineering; D016415:Sequence Alignment; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D005936:Glucans; D016695:Glycosyltransferases; D006026:Glycoside Hydrolases; C028020:licheninase