Literature summary for 2.3.1.180 extracted from

Qiu, X.; Janson, C.A.; Konstantinidis, A.K.; Nwagwu, S.; Silverman, C.; Smith, W.W.; Khandekar, S.; Lonsdale, J.; Abdel-Meguid, S.S.
Crystal structure of beta-ketoacyl-acyl carrier protein synthase III. A key condensing enzyme in bacterial fatty acid biosynthesis (1999), J. Biol. Chem., 274, 36465-36471.

Search for more literature for 2.3.1.180

Application

Application	Comment	Organism
pharmacology	the enzyme is a target for development of antibiotics	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified FabH as apoenzyme or with bound acetyl-CoA, structure and reaction mechanism modeling	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 a key catalyst of fatty acid biosynthesis	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
acetyl-CoA + a malonyl-[acyl-carrier protein] = an acetoacetyl-[acyl-carrier protein] + CoA + CO2	catalytic residues are Cys112, His244, and Asn274, catalytic reaction mechanism includes acetylation of Cys112 in the primer binding pocket, structure and reaction mechanism modeling	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme is a key catalyst of fatty acid biosynthesis	Escherichia coli	?	-	?

Subunits

Subunits	Comment	Organism
More	the enzyme shows a condensing enzyme fold	Escherichia coli

Synonyms

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)