The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

Accepted name: fatty acid kinase
Reaction: ATP + a fatty acid = ADP + a fatty acyl phosphate (overall reaction)
(1a) ATP + a fatty acid-[fatty acid-binding protein] = ADP + a fatty acyl phosphate-[fatty acid-binding protein]
(1b) a fatty acyl phosphate-[fatty acid-binding protein] + a fatty acid = a fatty acyl phosphate + a fatty acid-[fatty acid-binding protein]
Other name(s): fakAB (gene names)
Systematic name: ATP:fatty acid 1-phosphotransferase
Comments: The enzyme is a dimeric complex consisting of an ATP-binding protein (FakA) and a fatty acid-binding protein (FakB). The first step in the reaction is the binding of FakB (with a bound fatty acid) to FakA. The fatty acid bound to FakB is then phosphorylated by FakA, and the fatty acyl phosphate-bound FakB is released from the complex. In the presence of an exchangeable fatty acid pool in the cell membrane, the fatty acy phosphate bound to FakB exchanges with a fatty acid to regenerate the substrate for FakA. The system is widespread in Gram-positive bacteria, with most strains possessing a single FakA protein along with multiple FakB subunits that differ in their specificity towards fatty acid substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Parsons, J.B., Frank, M.W., Jackson, P., Subramanian, C. and Rock, C.O. Incorporation of extracellular fatty acids by a fatty acid kinase-dependent pathway in Staphylococcus aureus. Mol. Microbiol. 92 (2014) 234–245. [DOI] [PMID: 24673884]
2.  Parsons, J.B., Broussard, T.C., Bose, J.L., Rosch, J.W., Jackson, P., Subramanian, C. and Rock, C.O. Identification of a two-component fatty acid kinase responsible for host fatty acid incorporation by Staphylococcus aureus. Proc. Natl. Acad. Sci. USA 111 (2014) 10532–10537. [DOI] [PMID: 25002480]
3.  Broussard, T.C., Miller, D.J., Jackson, P., Nourse, A., White, S.W. and Rock, C.O. Biochemical roles for conserved residues in the bacterial fatty acid-binding protein family. J. Biol. Chem. 291 (2016) 6292–6303. [DOI] [PMID: 26774272]
[EC created 2021]

Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald