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Enzymatic activities of proteins encoded by PmurB, PmurC, and PmurE involved in methanogen pseudomurein biosynthesis

Guihong Cha1,2, Zhenli Lai3, Shuxin Wang3

  • 1School of Food and Liquor Engineering (School of Wuliangye Baijiu), Sichuan University of Science and Engineering, Yibin, China.

Frontiers in Microbiology
|March 20, 2026
PubMed

Insights

Researchers elucidated pseudomurein biosynthesis in methanogens by identifying key PMurBCE ligases. This discovery offers insights into cell wall synthesis and potential biotechnological applications against archaea.

Area of Science:

  • Biochemistry
  • Microbiology
  • Structural Biology

Background:

  • Pseudomurein is a cell wall glycan polymer found in Methanobacteriales and Methanopyrales.
  • Pseudomurein shares similarities with bacterial peptidoglycan but its biosynthesis is uncharacterized.

Purpose of the Study:

  • To identify and characterize enzymes involved in pseudomurein biosynthesis.
  • To elucidate the enzymatic activities of PMurBCE ligases in methanogens.

Main Methods:

  • Enzyme identification and characterization.
  • Structural model analysis of archaeal PMur enzymes.
  • Biochemical assays to determine enzyme function.

Main Results:

  • Key PMurBCE ligases were identified and their roles in peptide chain biosynthesis elucidated.
  • PMurB catalyzes UDP-Glu and Pi conjugation; PMurC adds alanine/threonine; PMurE adds lysine.
  • Structural analysis revealed similarities and substrate specificities between archaeal PMur and bacterial Mur ligases.

Conclusions:

  • The study provides the first detailed enzymatic mechanism for pseudomurein biosynthesis in methanogens.
  • Understanding pseudomurein synthesis opens avenues for biotechnological applications, including gene editing and novel antibacterial agents targeting methanogenic archaea.
Keywords:
PMur ligaseenzymatic activitiesmethanogenspseudomurein biosynthesisstructural

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