Literature summary for 2.3.1.180 extracted from

Alhamadsheh, M.; Musayev, F.; Komissarov, A.; Sachdeva, S.; Wright, H.; Scarsdale, N.; Florova, G.; Reynolds, K.
Alkyl-CoA disulfides as inhibitors and mechanistic probes for FabH enzymes (2007), Chem. Biol., 14, 513-524 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
enzyme in complex with inhibitor CoA methyldisulfide	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
CoA methyldisulfide	CoA methyldisulfide shows rapid inhibition of one monomer of FabH through formation of a methyl disulfide conjugate. Reaction of the second subunit with either MeSSCoA or acetyl-CoA is much slower. In the presence of malonyl-ACP, the acylation rate of the second subunit is restored to that of the native FabH	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A6R0	-	-

Synonyms

Synonyms	Comment	Organism
FabH	-	Escherichia coli

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.0571	-	pH 7.4, 23°C	Escherichia coli	CoA methyldisulfide

General Information

General Information	Comment	Organism
metabolism	catalytic model, a structurally disordered apo-ecFabH dimer orders on binding either the first substrate, acetyl-CoA, or the inhibitor MeSSCoA, and is restored to a disordered state on binding of malonyl-ACP	Escherichia coli

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Release 2023.1 (January 2023)