Literature summary for 2.3.1.41 extracted from

Kursula, P.; Sikkilae, H.; Fukao, T.; Kondo, N.; Wierenga, R.K.
High resolution crystal structures of human cytosolic thiolase (CT): A comparison of the active sites of human CT, bacterial thiolase, and bacterial KAS I (2005), J. Mol. Biol., 347, 189-201.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
comparison of crystal structures of the active sites of Escherichia coli KAS I with human cytosolic acetoacetyl-CoA thiolase and bacterial thiolase, overview	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A953	-	-

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]	catalytic active site residues are Cys163 and His333, the active site contains two oxyanion holes, stabilizing the thioester oxyanion of acetylated CoA and of acetylated Cys92, respectively	Escherichia coli	a

Subunits

Subunits	Comment	Organism
More	comparison of crystal structures of the active sites of Escherichia coli KAS I with human cytosolic acetoacetyl-CoA thiolase and bacterial thiolase, active sites with four highly conserved loop structures, overview	Escherichia coli

Synonyms

Synonyms	Comment	Organism
beta-ketoacyl ACP synthase I	-	Escherichia coli
KAS I	-	Escherichia coli
More	the enzyme belongs to the superfamily of condensing enzymes which includes thiolases	Escherichia coli

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Release 2023.1 (January 2023)