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Literature summary for 2.3.1.180 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

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
Escherichia coli
acetyl-CoA
-
Enterococcus faecalis

IC50 Value

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

General Information

General Information Comment Organism
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
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
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
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
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
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