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The evolution of acetyl-CoA synthase.

P A Lindahl1, B Chang

  • 1Departments of Chemistry and of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-3255, USA. Lindahl@mail.chem.tamu.edu

Origins of Life and Evolution of the Biosphere : the Journal of the International Society for the Study of the Origin of Life
|October 16, 2001
PubMed
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Acetyl-coenzyme A synthases (ACS) are crucial enzymes in archaea and bacteria. Phylogenetic analysis reveals evolutionary relationships among ACS subunits, aiding in understanding enzyme diversity and function.

Area of Science:

  • Biochemistry and enzymology
  • Microbial evolution
  • Bioinorganic chemistry

Background:

  • Acetyl-coenzyme A synthases (ACS) are nickel-iron-sulfur cluster enzymes vital for carbon metabolism in archaea and bacteria.
  • ACS enzymes are classified into four distinct classes (I-IV) based on their catalytic functions and subunit compositions.

Purpose of the Study:

  • To conduct a comprehensive phylogenetic analysis of all five ACS subunits (alpha, beta, gamma, delta, epsilon).
  • To identify conserved residues potentially involved in metal cluster ligation and catalytic activity across different ACS classes.
  • To elucidate the evolutionary history and functional diversification of ACS enzymes and their host organisms.

Main Methods:

  • Phylogenetic analysis of amino acid sequences for all five ACS subunits.

Related Experiment Videos

  • Identification and comparison of conserved residues across different ACS classes.
  • Comparative analysis of subunit sequence divergence and structural features.

    • Main Results:

    • ACS alpha subunit phylogeny clearly delineates Class I/II from Class III/IV-like sequences, suggesting it best reflects functional diversity.
    • Conserved residues potentially ligating B- and C-clusters were identified in alpha subunits; additional ligands for Class I/II enzymes were also found.
    • Beta subunit sequences showed less divergence than alpha, with unique N-terminal extensions in Class III-like beta subunits.
    • Gamma and delta subunits exhibited distinct phylogenetic groupings corresponding to ACS classes, while epsilon subunits showed high divergence.

    Conclusions:

    • The alpha subunit phylogeny provides the most robust framework for understanding ACS functional diversity and evolutionary relationships.
    • Conserved residues highlight key structural and functional elements, including metal cofactor binding sites.
    • The study provides insights into the evolutionary pathways of ACS enzymes and the organisms that utilize them.