Thiolase
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Thiolases, also known as acetyl-coenzyme A acetyltransferases (ACAT), are enzymes which convert two units of acetyl-CoA to acetoacetyl CoA in the mevalonate pathway.
Thiolase, N-terminal domain | |||||||||
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Identifiers | |||||||||
Symbol | Thiolase_N | ||||||||
Pfam | PF00108 | ||||||||
InterPro | IPR002155 | ||||||||
PROSITE | PDOC00092 | ||||||||
SCOP2 | 1pxt / SCOPe / SUPFAM | ||||||||
CDD | cd00751 | ||||||||
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Thiolase, C-terminal domain | |||||||||
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Identifiers | |||||||||
Symbol | Thiolase_C | ||||||||
Pfam | PF02803 | ||||||||
InterPro | IPR002155 | ||||||||
PROSITE | PDOC00092 | ||||||||
SCOP2 | 1pxt / SCOPe / SUPFAM | ||||||||
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Thiolases are ubiquitous enzymes that have key roles in many vital biochemical pathways, including the beta oxidation pathway of fatty acid degradation and various biosynthetic pathways.[1] Members of the thiolase family can be divided into two broad categories: degradative thiolases (EC 2.3.1.16) and biosynthetic thiolases (EC 2.3.1.9). These two different types of thiolase are found both in eukaryotes and in prokaryotes: acetoacetyl-CoA thiolase (EC:2.3.1.9) and 3-ketoacyl-CoA thiolase (EC:2.3.1.16). 3-ketoacyl-CoA thiolase (also called thiolase I) has a broad chain-length specificity for its substrates and is involved in degradative pathways such as fatty acid beta-oxidation. Acetoacetyl-CoA thiolase (also called thiolase II) is specific for the thiolysis of acetoacetyl-CoA and involved in biosynthetic pathways such as beta-hydroxybutyric acid synthesis or steroid biogenesis.
The formation of a carbon–carbon bond is a key step in the biosynthetic pathways by which fatty acids and polyketide are made. The thiolase superfamily enzymes catalyse the carbon–carbon-bond formation via a thioester-dependent Claisen condensation[2] reaction mechanism.[3]