ArticleThe Journal of biological chemistry2022
Domain architecture and catalysis of the Staphylococcus aureus fatty acid kinase.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Differential pathogenic and commensal response ofJournal of bacteriology · 2026Article
- Staphylococcus aureus fatty acid metabolism governs saeRS-mediated aggregation in joint infections.Nature communications · 2025Article
- Defining the Enterococcus faecalis Fatty Acid Kinase System of Exogeneous Fatty Acid Utilization.Molecular microbiology · 2025Article
- Phenotypic and genetic stepwise changes inAntimicrobial agents and chemotherapy · 2025Article
- Structure and catalytic mechanism of exogenous fatty acid recycling by AasS, a versatile acyl-ACP synthetase.Nature structural & molecular biology · 2025Article
- Bacterial acquisition of host fatty acids has far-reaching implications on virulence.Microbiology and molecular biology reviews : MMBR · 2024Review
- Review
- Structure and mechanism for streptococcal fatty acid kinase (Fak) system dedicated to host fatty acid scavenging.Science advances · 2022Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Fatty acid kinase (Fak) is a two-component enzyme that generates acyl-phosphate for phospholipid synthesis. Fak consists of a kinase domain protein (FakA) that phosphorylates a fatty acid enveloped by a fatty acid binding protein (FakB). The structural basis for FakB function has been established, but little is known about FakA. Here, we used limited proteolysis to define three separate FakA domains: the amino terminal FakA_N, the central FakA_L, and the carboxy terminal FakA_C. The isolated domains lack kinase activity, but activity is restored when FakA_N and FakA_L are present individually or connected as FakA_NL. The X-ray structure of the monomeric FakA_N captures the product complex with ADP and two Mg
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Registered trials
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