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 | 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 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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A6R0 | - |
- |
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 | Comment | Organism |
---|---|---|
beta-ketoacyl-ACP-synthase III | - |
Escherichia coli |
FabH | - |
Escherichia coli |
fatty acid biosynthesis, enzyme H | - |
Escherichia coli |
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 |