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Literature summary for 2.3.1.41 extracted from

  • Price, A.C.; Choi, K.H.; Heath, R.J.; Li, Z.; White, S.W.; Rock, C.O.
    Inhibition of beta-ketoacyl-acyl carrier protein synthases by thiolactomycin and cerulenin. Structure and mechanism (2001), J. Biol. Chem., 276, 6551-6559.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
synthases I, II, and III, recombinant expression Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
structure analysis, three-dimensional model of enzyme complexed with inhibitors thiolactomycin and cerulenin Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
cerulenin analysis of the binding mechanism, mimicks the condensation transition state; FabB: inhibition is irreversible Escherichia coli
thiolactomycin analysis of the binding mechanism, mimics malonyl-[acyl-carrier-protein]; FabB: inhibition is reversible, competitive Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
synthases I, II, and III
-

Purification (Commentary)

Purification (Comment) Organism
recombinant synthases I, i.e. FabA, II, i.e. FabB, and III, i.e.FabH Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein] synthaseIII/FabH: His-Asn-Cys catalytic triad Escherichia coli
an acyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a 3-oxoacyl-[acyl-carrier protein] + CO2 + an [acyl-carrier protein] synthaseII/FabB: His-HIs-Cys catalytic triad Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
saturated acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein]
-
Escherichia coli 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]
-
?