Application | Comment | Organism |
---|---|---|
drug development | the enzyme is a promising target for the development of therapeutic agents | Yersinia pestis |
Cloned (Comment) | Organism |
---|---|
gene fabF, recombinant expression of N-terminally His6-tagged enzyme with a TEV protease cleavage site in Escherichia coli strain BL21(DE3) pLysS | Yersinia pestis |
Crystallization (Comment) | Organism |
---|---|
purified recombinant enzyme, hanging drop vapour diffusion technique, mixing of 0.0015 ml of 21 mg/ml protein solution with an equal amount of reservoir solution, containing 0.2 M lithium chloride, 0.1 M HEPES sodium salt pH 7.0, and 24% PEG 6000, and equilibration against 0.3 ml of reservoir solution, 13°C, X-ray diffraction structure determination and analysis at 2.7 A resolution, molecular replacement using the enzyme structure of Escherichia coli, PDB ID 1KAS, as search model | Yersinia pestis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
cerulenin | - |
Yersinia pestis | |
additional information | inhibitor interaction with the active site, structure analysis, docking study, overview | Yersinia pestis | |
platencin | - |
Yersinia pestis | |
platensimycin | - |
Yersinia pestis | |
thiolactomycin | - |
Yersinia pestis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Yersinia pestis | Q7CJ22 | gene fabF | - |
Purification (Comment) | Organism |
---|---|
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) pLysS by nickel affinty chromatography, tag cleavage by TEV protease, gel filtration, and ultrafiltration to over 90% purity | Yersinia pestis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
a (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein] | two-stage mechanism, driven by a dipole moment, the active site cysteine, Cys164 in YpFabF attacks the acyl group of a fatty acyl donor, transferring the acyl group to the enzyme. The bound fatty acyl donor molecule is displaced, and the receiving molecule or fatty acyl thioester to be elongated binds, initiating the transfer of the acyl group from the condensing enzyme to the recipient. The remaining residues of the catalytic triad, His304 and His341, are thought to stabilise the fatty acyl intermediate during transition states | Yersinia pestis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | enzyme substrate specificity, overview | Yersinia pestis | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | the YpFabF monomer contains 13 alpha-helices and 14 beta-strands, the core motif of YpFabF contains a characteristic thiolase fold, dimer interface structure, structure comparison with FabH, EC 2.3.1.180 | Yersinia pestis |
Synonyms | Comment | Organism |
---|---|---|
beta-ketoacyl-acyl carrier protein synthase II | - |
Yersinia pestis |
FabF | - |
Yersinia pestis |
General Information | Comment | Organism |
---|---|---|
metabolism | the beta-ketoacyl-acyl carrier protein (ACP) synthases, FabB, FabF, and FabH, catalyse the Claisen condensation of fatty acyl-thioesters and malonyl-ACP to form a 3-oxoacyl-ACP intermediate elongated by two carbon atoms. The initial cycle of elongation is catalysed by FabH, involving condensation of malonyl-ACP and acetyl-CoA, while subsequent cycles of elongation are performed by FabB or FabF | Yersinia pestis |
additional information | enzyme structure and active site architecture, comparison with FabH, EC 2.3.1.180. Substrate binding is controlled by residue Phe401 | Yersinia pestis |