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Literature summary for 2.3.1.179 extracted from

  • Nanson, J.D.; Himiari, Z.; Swarbrick, C.M.; Forwood, J.K.
    Structural characterisation of the beta-ketoacyl-acyl carrier protein synthases, FabF and FabH, of Yersinia pestis (2015), Sci. Rep., 5, 14797.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
drug development the enzyme is a promising target for the development of therapeutic agents Yersinia pestis

Cloned(Commentary)

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 (Commentary)

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

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

Organism UniProt Comment Textmining
Yersinia pestis Q7CJ22 gene fabF
-

Purification (Commentary)

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

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 and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme substrate specificity, overview Yersinia pestis ?
-
?

Subunits

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

Synonyms Comment Organism
beta-ketoacyl-acyl carrier protein synthase II
-
Yersinia pestis
FabF
-
Yersinia pestis

General Information

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