PMID: 11934493Apr 6, 2002Paper

Pseudomurein endoisopeptidases PeiW and PeiP, two moderately related members of a novel family of proteases produced in Methanothermobacter strains

FEMS Microbiology Letters
Yongneng LuoA Wasserfallen

Abstract

Sequence comparison of pseudomurein endoisopeptidases PeiW encoded by the defective prophage PsiM100 of Methanothermobacter wolfeii, and PeiP encoded by phage PsiM2 of Methanothermobacter marburgensis, revealed that the two enzymes share only limited similarity. Their amino acid sequences comprise an N-terminal domain characterized by the presence of direct repeats and a C-terminal domain with a catalytic triad C-H-D as in thiol proteases and animal transglutaminases. Both PeiW and PeiP catalyze the in vitro lysis of M. marburgensis cells under reducing conditions and exhibit characteristics of metal-activated peptidases. Optimal temperature and pH were determined to be 63 degrees C and 6.4 for His-tagged PeiP and 71 degrees C and 6.4 for His-tagged PeiW, respectively. Database search results suggest that PeiW and PeiP are the first two experimentally identified members of a novel family of proteases in a superfamily of archaeal, bacterial, and eukaryotic protein homologs of animal transglutaminases.

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Citations

Nov 30, 2010·Archaea : an International Microbiological Journal·Ganesh Ram R VisweswaranJan Kok
Oct 21, 2011·Applied Microbiology and Biotechnology·Ganesh Ram R VisweswaranJan Kok
Nov 21, 2007·Journal of Microbiological Methods·Kengo KubotaAkiyoshi Ohashi
Oct 21, 2015·Archaea : an International Microbiological Journal·Linley R SchofieldRon S Ronimus
Jun 28, 2005·Current Opinion in Microbiology·Martin J Loessner
Apr 12, 2007·Molecular Microbiology·Peter J M SteenbakkersJan T Keltjens
Nov 11, 2017·Nature Reviews. Microbiology·David PrangishviliMart Krupovic
Aug 5, 2019·Biochimie·Neil D Rawlings, Alex Bateman

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