Interfacial Enzymes Enable Gram-Positive Microbes to Eat Fatty Acids

Research output: Contribution to journalReview articlepeer-review

1 Scopus citations


Exogenous fatty acid (eFA) activation and utilization play key roles in bacterial physiology and confer growth advantages by bypassing the need to make fatty acids for lipid synthesis. In Gram-positive bacteria, eFA activation and utilization is generally carried out by the fatty acid kinase (FakAB) two-component system that converts eFA to acyl phosphate, and the acyl-ACP:phosphate transacylase (PlsX) that catalyzes the reversible conversion of acyl phosphate to acyl–acyl carrier protein. Acyl–acyl carrier protein is a soluble format of the fatty acid that is compatible with cellular metabolic enzymes and can feed multiple processes including the fatty acid biosynthesis pathway. The combination of FakAB and PlsX enables the bacteria to channel eFA nutrients. These key enzymes are peripheral membrane interfacial proteins that associate with the membrane through amphipathic helices and hydrophobic loops. In this review, we discuss the biochemical and biophysical advances that have established the structural features that drive FakB or PlsX association with the membrane, and how these protein–lipid interactions contribute to enzyme catalysis.

Original languageEnglish
Article number423
Issue number4
StatePublished - Apr 2023

Bibliographical note

Funding Information:
This work was supported by the National Institutes of Health, United States grant 1K99AI166116. The content is solely the responsibility of the author and does not necessarily represent the official views of the National Institutes of Health.

Publisher Copyright:
© 2023 by the author.


  • fatty acid metabolism
  • interfacial enzymes
  • mechanism
  • membrane binding
  • peripheral membrane proteins

ASJC Scopus subject areas

  • Chemical Engineering (miscellaneous)
  • Process Chemistry and Technology
  • Filtration and Separation


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