Oberbarnscheidt, Leoni and Taylor, Edward J. and Davies, Gideon J. and Gloster, Tracey M. (2007) Structure of a carbohydrate esterase from Bacillus anthracis. PROTEINS: Structure, Function, and Bioinformatics, 66 (1). pp. 250-252. ISSN 1097-0134

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Abstract

Family 4 carbohydrate esterases (CEs) catalyse the N- or O-deacetylation of substrates such as acetylated xylan, chitin, and peptidoglycan. CEs are classified into 14 families by sequence homology (see http://afmb.cnrs-mrs.fr/CAZY1). Family 4 is by far the largest of the CE families, with over 1000 open reading frames. The structure of CE4 enzymes from a number of bacterial species have been solved, including the peptidoglycan deacetylases from Streptococcus pneumoniae and Bacillus subtilis,3 acetyl xylan esterases from Clostridium thermocellum and Streptomyces lividans,4 and an enzyme of unknown specificity from Pseudomonas aeruginosa (PDBcode 1Z7A). CE4 enzymes contain a conserved NodB homology domain, and adopt a distorted (a/b)8 barrel fold. Most of the structures contain a divalent ion in the active site that is necessary for enzyme activity2,4 and which is coordinated by highly conserved histidine and aspartate residues.

Item Type:	Article
Additional Information:	Family 4 carbohydrate esterases (CEs) catalyse the N- or O-deacetylation of substrates such as acetylated xylan, chitin, and peptidoglycan. CEs are classified into 14 families by sequence homology (see http://afmb.cnrs-mrs.fr/CAZY1). Family 4 is by far the largest of the CE families, with over 1000 open reading frames. The structure of CE4 enzymes from a number of bacterial species have been solved, including the peptidoglycan deacetylases from Streptococcus pneumoniae and Bacillus subtilis,3 acetyl xylan esterases from Clostridium thermocellum and Streptomyces lividans,4 and an enzyme of unknown specificity from Pseudomonas aeruginosa (PDBcode 1Z7A). CE4 enzymes contain a conserved NodB homology domain, and adopt a distorted (a/b)8 barrel fold. Most of the structures contain a divalent ion in the active site that is necessary for enzyme activity2,4 and which is coordinated by highly conserved histidine and aspartate residues.
Keywords:	Family 4 carbohydrate esterases, conserved histidine and aspartate
Subjects:	C Biological Sciences > C700 Molecular Biology, Biophysics and Biochemistry
Divisions:	College of Sciences > Faculty of Science > School of Life Sciences
Depositing User:	Edward Taylor
Date Deposited:	18 Sep 2012 20:08
Last Modified:	13 Mar 2013 09:13
URI:	http://eprints.lincoln.ac.uk/id/eprint/6160

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