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

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The crystal structure of a family GH25 lysozyme from Bacillus anthracis implies a neighboring-group catalytic mechanism with retention of anomeric configuration. / Martinez-Fleites, Carlos; Korczynska, Justyna E.; Davies, Gideon J.; Cope, Matthew J.; Turkenburg, Johan P.; Taylor, Edward J.

In: CARBOHYDRATE RESEARCH, Vol. 344, No. 13, 08.09.2009, p. 1753-1757.

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Harvard

Martinez-Fleites, C, Korczynska, JE, Davies, GJ, Cope, MJ, Turkenburg, JP & Taylor, EJ 2009, 'The crystal structure of a family GH25 lysozyme from Bacillus anthracis implies a neighboring-group catalytic mechanism with retention of anomeric configuration', CARBOHYDRATE RESEARCH, vol. 344, no. 13, pp. 1753-1757. https://doi.org/10.1016/j.carres.2009.06.001

APA

Martinez-Fleites, C., Korczynska, J. E., Davies, G. J., Cope, M. J., Turkenburg, J. P., & Taylor, E. J. (2009). The crystal structure of a family GH25 lysozyme from Bacillus anthracis implies a neighboring-group catalytic mechanism with retention of anomeric configuration. CARBOHYDRATE RESEARCH, 344(13), 1753-1757. https://doi.org/10.1016/j.carres.2009.06.001

Vancouver

Martinez-Fleites C, Korczynska JE, Davies GJ, Cope MJ, Turkenburg JP, Taylor EJ. The crystal structure of a family GH25 lysozyme from Bacillus anthracis implies a neighboring-group catalytic mechanism with retention of anomeric configuration. CARBOHYDRATE RESEARCH. 2009 Sep 8;344(13):1753-1757. https://doi.org/10.1016/j.carres.2009.06.001

Author

Martinez-Fleites, Carlos ; Korczynska, Justyna E. ; Davies, Gideon J. ; Cope, Matthew J. ; Turkenburg, Johan P. ; Taylor, Edward J. / The crystal structure of a family GH25 lysozyme from Bacillus anthracis implies a neighboring-group catalytic mechanism with retention of anomeric configuration. In: CARBOHYDRATE RESEARCH. 2009 ; Vol. 344, No. 13. pp. 1753-1757.

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@article{1ec9934d4c274d39a77cc4f7f075f9f5,
title = "The crystal structure of a family GH25 lysozyme from Bacillus anthracis implies a neighboring-group catalytic mechanism with retention of anomeric configuration",
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 (alpha/beta)(5)(beta)(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 angstrom resolution. We show that the active center is extremely similar 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. (C) 2009 Elsevier Ltd. All rights reserved.",
keywords = "Lysozyme, Autolysin, Peptidoglycan cleavage, Anthrax, Hexosaminidase, SUBSTRATE-ASSISTED CATALYSIS, PHAGE LYTIC ENZYME, ACTIVE-SITE, MOLECULAR REPLACEMENT, GLYCOSYL HYDROLASES, MUREIN HYDROLASES, CELL-WALL, IDENTIFICATION, RECOGNITION, CHITOBIASE",
author = "Carlos Martinez-Fleites and Korczynska, {Justyna E.} and Davies, {Gideon J.} and Cope, {Matthew J.} and Turkenburg, {Johan P.} and Taylor, {Edward J.}",
year = "2009",
month = "9",
day = "8",
doi = "10.1016/j.carres.2009.06.001",
language = "English",
volume = "344",
pages = "1753--1757",
journal = "CARBOHYDRATE RESEARCH",
issn = "0008-6215",
publisher = "Elsevier BV",
number = "13",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - The crystal structure of a family GH25 lysozyme from Bacillus anthracis implies a neighboring-group catalytic mechanism with retention of anomeric configuration

AU - Martinez-Fleites, Carlos

AU - Korczynska, Justyna E.

AU - Davies, Gideon J.

AU - Cope, Matthew J.

AU - Turkenburg, Johan P.

AU - Taylor, Edward J.

PY - 2009/9/8

Y1 - 2009/9/8

N2 - 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 (alpha/beta)(5)(beta)(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 angstrom resolution. We show that the active center is extremely similar 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. (C) 2009 Elsevier Ltd. All rights reserved.

AB - 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 (alpha/beta)(5)(beta)(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 angstrom resolution. We show that the active center is extremely similar 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. (C) 2009 Elsevier Ltd. All rights reserved.

KW - Lysozyme

KW - Autolysin

KW - Peptidoglycan cleavage

KW - Anthrax

KW - Hexosaminidase

KW - SUBSTRATE-ASSISTED CATALYSIS

KW - PHAGE LYTIC ENZYME

KW - ACTIVE-SITE

KW - MOLECULAR REPLACEMENT

KW - GLYCOSYL HYDROLASES

KW - MUREIN HYDROLASES

KW - CELL-WALL

KW - IDENTIFICATION

KW - RECOGNITION

KW - CHITOBIASE

UR - http://www.scopus.com/inward/record.url?scp=68949170989&partnerID=8YFLogxK

U2 - 10.1016/j.carres.2009.06.001

DO - 10.1016/j.carres.2009.06.001

M3 - Article

VL - 344

SP - 1753

EP - 1757

JO - CARBOHYDRATE RESEARCH

JF - CARBOHYDRATE RESEARCH

SN - 0008-6215

IS - 13

ER -