Literature summary for 2.3.1.9 extracted from

Haapalainen, A.M.; Merilaeinen, G.; Pirilae, P.L.; Kondo, N.; Fukao, T.; Wierenga, R.K.
Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase: the importance of potassium and chloride ions for its structure and function (2007), Biochemistry, 46, 4305-4321.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method at 4°C. Unliganded and liganded (with CoA and with K+) structures of the human mitochondrial recombinant tetrameric thiolase	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Homo sapiens	5739	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cl-	the crystal structures of T2 show that each T2 subunit has a binding site for a chloride ion and a potassium ion. Each of these ion binding sites is defined well by loops at the active site, resulting in the stabilization of the catalytic loops	Homo sapiens
K+	the crystal structures of T2 show that each T2 subunit has a binding site for a chloride ion and a potassium ion. Each of these ion binding sites is defined well by loops at the active site, resulting in the stabilization of the catalytic loops	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetyl-CoA + acetyl-CoA	-	Homo sapiens	CoA + acetoacetyl-CoA	-	?

Synonyms

Synonyms	Comment	Organism
acetoacetyl-CoA thiolase	-	Homo sapiens

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Release 2023.1 (January 2023)