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- Title
The acyl carrier proteins of lipid synthesis are busy having other affairs.
- Authors
Cronan, John E.
- Abstract
This is a review of the acyl carrier proteins (ACPs) of type II fatty acid synthesis in bacteria and mitochondria, their structures and protein interactions. Type II fatty acid synthesis in bacteria (Prog. Lipid Res. (2013) 52, 249–276; Biochim. Biophys. Acta (1996) 1302, 1–16; Annu. Rev. Biochem. (2005) 74, 791–831) and in the mitochondria of yeast and mammals (Biochim. Biophys. Acta Mol. Cell. Res. (2019) 1866, 118540; MedChemComm (2019) 10, 209–220; Elife (2016) 5, e17828; Mol. Cell (2018) 71, 567–580.e4) will be discussed only tangentially in this review. The above references are excellent recent reviews. Bacterial fatty acid synthesis has been a popular target for the development of new antimicrobials and an up-to-date review of the field has been published (Annu. Rev. Microbiol. (2022) 76, 281–304). The ACP-like proteins of secondary metabolites (e.g. polyketide synthesis will not be reviewed). Escherichia coli ACP is now called AcpP to distinguish it from the enzymes that attach (AcpS) and remove (AcpH) the 40 -phosphopantetheine (40 PP) prosthetic group. Note that the primary translation product of the acpP gene is called apoAcpP. The addition of the 40 PP prosthetic group converts apo-AcpP to holo-AcpP (commonly referred to as AcpP). Acylation of the 40 PP prosthetic group gives acyl-AcpP species. The length of the acyl chain determines the properties of the acyl-AcpP as will be discussed below.
- Subjects
ACYL carrier protein; LIPID synthesis; PROTEIN synthesis; METABOLITES; POLYKETIDES; PROTEIN structure; PLANT mitochondria
- Publication
Biochemical Journal, 2023, Vol 480, Issue 12, p855
- ISSN
0264-6021
- Publication type
Article
- DOI
10.1042/BCJ20230161