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Volume 2010 (2010), Article ID 480492, 4 pages
Review Article

Two Major Archaeal Pseudomurein Endoisopeptidases: PeiW and PeiP

1Department of Molecular Genetics, GBB, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands
2Laboratory of Biophysical Chemistry, GBB, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands

Received 30 June 2010; Accepted 8 October 2010

Academic Editor: William B. Whitman

Copyright © 2010 Ganesh Ram R. Visweswaran et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


PeiW (UniProtKB Q7LYX0) and PeiP (UniProtKB Q77WJ4) are the two major pseudomurein endoisopeptidases (Pei) that are known to cleave pseudomurein cell-wall sacculi of the members of the methanogenic orders Methanobacteriales and Methanopyrales. Both enzymes, originating from prophages specific for some methanogenic archaeal species, hydrolyze the 𝜀 (Ala)-Lys bond of the peptide linker between adjacent pseudomurein layers. Because lysozyme is not able to cleave the pseudomurein cell wall, the enzymes are used in protoplast preparation and in DNA isolation from pseudomurein cell-wall-containing methanogens. Moreover, PeiW increases the probe permeability ratio and enables fluorescence in situ hybridization (FISH) and catalyzed reporter deposition (CARD-) FISH experiments to be performed on these methanogens.