Literature summary for 2.3.1.180 extracted from

Qiu, X.; Janson, C.A.; Smith, W.W.; Head, M.; Lonsdale, J.; Konstantinidis, A.K.
Refined structures of beta-ketoacyl-acyl carrier protein synthase III (2001), J. Mol. Biol., 307, 341-356.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
purified FabH as apoenzyme or ligand-bound complex, X-ray diffraction structure determination and analysis at 1.46 A resolution	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Escherichia coli	the enzyme is important in fatty acid biosynthesis	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A6R0	gene fabH	-

Reaction

Reaction	Comment	Organism	Reaction ID
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	catalytic reaction mechanism might include a water molecule or a hydroxyl anion in Cys112 deprotonation, large conformational changes in the active site e.g. through disordering of four essential loops and the movement of the two catalytic residues Cys112 and His244	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme is important in fatty acid biosynthesis	Escherichia coli	?	-	?

Subunits

Subunits	Comment	Organism
More	three-dimensional structure analysis, the enzyme contains a large solvent-accessible channel in the dimer interface as well as two cis-peptides, cis-Pro88 and cis-Phe308, in two of the disordered loops, structural instability	Escherichia coli

Synonyms

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

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Release 2023.1 (January 2023)