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Literature summary for 2.3.1.180 extracted from

  • Ramamoorthy, D.; Turos, E.; Guida, W.C.
    Identification of a new binding site in E. coli FabH using molecular dynamics simulations: validation by computational alanine mutagenesis and docking studies (2013), J. Chem. Inf. Model., 53, 1138-1156.
    View publication on PubMed
Search for more literature for 2.3.1.180

Application

Application Comment Organism
drug development the enzyme is a potential target for anti-infection drug discovery, the dimer interface in FabH is potentially a viable target for designing another class of inhibitors Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
additional information the dimer interface could be a potential target for anti-infection drug discovery, structure-based inhibitor design, overview. Cerulenin is no inhibitor of FabH Escherichia coli
platencin a dual inhibitor of FabH and FabF/FabB Escherichia coli
thiolactomycin specific for FabH Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
 2 * 35000, structural details of the dimer interface region by means of computational modeling, including molecular dynamics simulations, overview Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A6R0
-
-

Subunits

Subunits Comment Organism
homodimer 2 * 35000, structural details of the dimer interface region by means of computational modeling, including molecular dynamics simulations, overview Escherichia coli
More structural details of the dimer interface region by means of computational modeling, including molecular dynamics simulations, detailed overview. Residues required for intersubunit stability are Phe87 and its complementary residues from the adjacent monomer, Thr190, Leu191, Pro192, Asn193. The active site is composed of a catalytic triad formed by residues, Cys112, His244, and Asn274. Residue Cys112 is involved in acetyl transfer, while His244 and Asn274 play an active role in decarboxylation. Residues His244 and Asn274 are present close to Cys112 in the long active site tunnel. Cysteine 112 lies on the bottom of the active-site tunnel, the entrance of which is flanked by residues Trp32 and Arg151 Escherichia coli

Synonyms

Synonyms Comment Organism
beta-ketoacyl-ACP-synthase III
-
 Escherichia coli
FabH
-
 Escherichia coli
fatty acid biosynthesis, enzyme H
-
 Escherichia coli

General Information

General Information Comment Organism
metabolism FabB, FabF, and FabH are the condensing enzymes in te fatty acid synthesis system FAS II that play an important role in the initiation and elongation of fatty acid chains. FabB and FabF use acyl-ACPs as primers, while FabH uses acetyl-CoA as an acyl donor, which makes it unique among the FAS II condensing enymes Escherichia coli
physiological function beta-ketoacyl-ACP-synthase III is a key condensing enzyme in the type II fatty acid synthesis system. The pathway in bacteria is essential for growth and survival Escherichia coli