ArticleArchaea (Vancouver, B.C.)2015
Biochemical Characterisation of Phage Pseudomurein Endoisopeptidases PeiW and PeiP Using Synthetic Peptides.
Article in Archaea (Vancouver, B.C.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Structural characterisation of nucleotide sugar short-chain dehydrogenases/reductases from the thermophilic pseudomurein-containing methanogen Methanothermobacter thermautotrophicus ΔH.The FEBS journal · 2026Article
- Stable coexistence between an archaeal virus and the dominant methanogen of the human gut.Nature communications · 2024Article
- Structural and mechanistic basis of the central energy-converting methyltransferase complex of methanogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- Hypersaline Lake Urmia: a potential hotspot for microbial genomic variation.Scientific reports · 2023Article
- Tailored Nanoparticles With the Potential to Reduce Ruminant Methane Emissions.Frontiers in microbiology · 2022Article
- Archaeal pseudomurein and bacterial murein cell wall biosynthesis share a common evolutionary ancestry.FEMS microbes · 2021Article
- Rumen Virus Populations: Technological Advances Enhancing Current Understanding.Frontiers in microbiology · 2020Review
- Inhibition of Rumen Methanogens by a Novel Archaeal Lytic Enzyme Displayed on Tailored Bionanoparticles.Frontiers in microbiology · 2018Article
- Expression, Purification, and Characterization of (Archaea (Vancouver, B.C.) · 2017Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pseudomurein endoisopeptidases cause lysis of the cell walls of methanogens by cleaving the isopeptide bond Ala-ε-Lys in the peptide chain of pseudomurein. PeiW and PeiP are two thermostable pseudomurein endoisopeptidases encoded by phage ΨM100 of Methanothermobacter wolfei and phages ΨM1 and ΨM2 of Methanothermobacter marburgensis, respectively. A continuous assay using synthetic peptide substrates was developed and used in the biochemical characterisation of recombinant PeiW and PeiP. The advantages of these synthetic peptide substrates over natural substrates are sensitivity, high purity, and characterisation and the fact that they are more easily obtained than natural substrates. In the presence of a reducing agent, purified PeiW and PeiP each showed similar activity under aerobic and anaerobic conditions. Both enzymes required a divalent metal for activity and showed greater thermostability in the presence of Ca(2+). PeiW and PeiP involve a cysteine residue in catalysis and have a monomeric native conformation. The kinetic parameters, K(M) and k(cat), were determined, and the ε-isopeptide bond between alanine and lysine was confirmed as the bond lysed by these enzymes in pseudomurein. The new assay may have wider applications for the general study of peptidases and the identification of specific methanogens susceptible to lysis by specific pseudomurein endoisopeptidases.
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