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Literature summary extracted from

  • Mittal, A.; Johnson, M.E.
    Conformational diversity of bacterial FabH: implications for molecular recognition specificity (2015), J. Mol. Graph. Model., 55, 115-122.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.180 2-((4-bromo-3-[(diethylamino)sulfonyl]benzoyl)amino)benzoic acid benzoylamino-benzoic acid derivative inhibitor-enzyme interaction analysis, overview Enterococcus faecalis
2.3.1.180 additional information indole analogue inhibitor-enzyme interaction analysis, overview Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] Escherichia coli
-
 an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] Enterococcus faecalis
-
 an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein] Enterococcus faecalis ATCC 700802
-
 an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.180 Enterococcus faecalis Q820T1 gene fabH
-
2.3.1.180 Enterococcus faecalis ATCC 700802 Q820T1 gene fabH
-
2.3.1.180 Escherichia coli P0A6R0
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein]
-
 Escherichia coli an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein]
-
 Enterococcus faecalis an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?
2.3.1.180 acetyl-CoA + a malonyl-[acyl-carrier protein]
-
 Enterococcus faecalis ATCC 700802 an acetoacetyl-[acyl-carrier protein] + CoA + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.180 beta-ketoacyl-acyl carrier protein synthase III
-
 Escherichia coli
2.3.1.180 beta-ketoacyl-acyl carrier protein synthase III
-
 Enterococcus faecalis
2.3.1.180 FabH
-
 Escherichia coli
2.3.1.180 FabH
-
 Enterococcus faecalis

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.180 acetyl-CoA
-
 Escherichia coli
2.3.1.180 acetyl-CoA
-
 Enterococcus faecalis

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.3.1.180 0.0016
-
 pH and temperature not specified in the publication Enterococcus faecalis 2-((4-bromo-3-[(diethylamino)sulfonyl]benzoyl)amino)benzoic acid

General Information

EC Number General Information Comment Organism
2.3.1.180 evolution enzymes FabH from Gram-positive and Gram-negative bacteria are known to have distinct preferences for acyl-CoA primers. This is functionally important, as the substrate specificity of the enzyme governs the fatty acid profile of the organism. FabH from Escherichia coli and other Gram-negative organisms are selective for acetyl-CoA and produce straight-chain fatty acids, while the FabH enzymes of Gram-positive bacteria such as bacilli prefer branched-chain primers and produce branched-chain fatty acids Escherichia coli
2.3.1.180 evolution enzymes FabH from Gram-positive and Gram-negative bacteria are known to have distinct preferences for acyl-CoA primers. This is functionally important, as the substrate specificity of the enzyme governs the fatty acid profile of the organism. FabH from Escherichia coli and other Gram-negative organisms are selective for acetyl-CoA and produce straight-chain fatty acids, while the FabH enzymes of Gram-positive bacteria such as bacilli prefer branched-chain primers and produce branched-chain fatty acids Enterococcus faecalis
2.3.1.180 additional information molecular dynamics simulations to characterize the conformational space accessible to enzyme homologues under native conditions, using the FabH crystal structure PDB ID 1MZS, with a bound indole analogue inhibitor, to start. Analysis of protein-ligand interactions in the ecFabH co-crystal structure Escherichia coli
2.3.1.180 additional information molecular dynamics simulations to characterize the conformational space accessible to enzyme homologues under native conditions, using the FabH crystal structure PDB ID 3IL5 to start. Analysis of protein-ligand interactions in the efFabH co-crystal structure Enterococcus faecalis
2.3.1.180 physiological function beta-ketoacyl-acyl carrier protein synthase III (FabH) is an essential enzyme in the FASII pathway, which catalyzes the first step in the pathway, the condensation of acyl-CoA primers with malonyl-ACP Escherichia coli
2.3.1.180 physiological function beta-ketoacyl-acyl carrier protein synthase III (FabH) is an essential enzyme in the FASII pathway, which catalyzes the first step in the pathway, the condensation of acyl-CoA primers with malonyl-ACP Enterococcus faecalis