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pubmed-article:10545327pubmed:abstractTextThiolases are ubiquitous and form a large family of dimeric or tetrameric enzymes with a conserved, five-layered alphabetaalphabetaalpha catalytic domain. Thiolases can function either degradatively, in the beta-oxidation pathway of fatty acids, or biosynthetically. Biosynthetic thiolases catalyze the biological Claisen condensation of two molecules of acetyl-CoA to form acetoacetyl-CoA. This is one of the fundamental categories of carbon skeletal assembly patterns in biological systems and is the first step in a wide range of biosynthetic pathways, including those that generate cholesterol, steroid hormones, and various energy-storage molecules.lld:pubmed
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pubmed-article:10545327pubmed:articleTitleA biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism.lld:pubmed
pubmed-article:10545327pubmed:affiliationEuropean Molecular Biology Laboratory, Postfach 10.2209, D-69012, Heidelberg, Germany.lld:pubmed
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