The crystal structure of a family GH25 lysozyme from Aspergillus fumigatus implies a neighboring-group catalytic mechanism with retention of anomeric configuration

Martinez-Fleites, Carlos and Korczynska, Justyna E. and Davies, Gideon J. and Cope, Matthew J. and Turkenburg, Johan P. and Taylor, Edward J. (2009) The crystal structure of a family GH25 lysozyme from Aspergillus fumigatus implies a neighboring-group catalytic mechanism with retention of anomeric configuration. Carbohydrate Research, 344 (13). pp. 1753-1757. ISSN 0008-6215

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Official URL: http://dx.doi.org/10.1016/j.carres.2009.06.001

Abstract

Lysozymes are found in many of the sequence-based families of glycoside hydrolases (www.cazy.org)
where they show considerable structural and mechanistic diversity. Lysozymes from glycoside hydrolase
family GH25 adopt a (a/b)5(b)3-barrel-like fold with a proposal in the literature that these enzymes act
with inversion of anomeric configuration; the lack of a suitable substrate, however, means that no group
has successfully demonstrated the configuration of the product. Here we report the 3-D structure of the
GH25 enzyme from Bacillus anthracis at 1.4 Å resolution. We show that the active center is extremely sim-
ilar to those from glycoside hydrolase families GH18, GH20, GH56, GH84, and GH85 implying that, in the
absence of evidence to the contrary, GH25 enzymes also act with net retention of anomeric configuration
using the neighboring-group catalytic mechanism that is common to this ‘super-family’ of enzymes

Item Type:Article
Additional Information:Lysozymes are found in many of the sequence-based families of glycoside hydrolases (www.cazy.org) where they show considerable structural and mechanistic diversity. Lysozymes from glycoside hydrolase family GH25 adopt a (a/b)5(b)3-barrel-like fold with a proposal in the literature that these enzymes act with inversion of anomeric configuration; the lack of a suitable substrate, however, means that no group has successfully demonstrated the configuration of the product. Here we report the 3-D structure of the GH25 enzyme from Bacillus anthracis at 1.4 Å resolution. We show that the active center is extremely sim- ilar to those from glycoside hydrolase families GH18, GH20, GH56, GH84, and GH85 implying that, in the absence of evidence to the contrary, GH25 enzymes also act with net retention of anomeric configuration using the neighboring-group catalytic mechanism that is common to this ‘super-family’ of enzymes
Keywords:fungal GH25, peptidoglycan cleavage, lysins, lysozomes
Subjects:C Biological Sciences > C790 Molecular Biology, Biophysics and Biochemistry not elsewhere classified
Divisions:College of Science > School of Life Sciences
ID Code:6122
Deposited By: Edward Taylor
Deposited On:08 Sep 2012 06:38
Last Modified:13 Mar 2013 09:13

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