<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Han S</submitter><funding>NIDDK NIH HHS</funding><pagination>2620-31</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3494255</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>53(12)</volume><pubmed_abstract>Thioesterase superfamily member 1 (Them1; synonyms acyl-CoA thioesterase 11 and StarD14) is highly expressed in brown adipose tissue and limits energy expenditure in mice. Them1 is a putative fatty acyl-CoA thioesterase that comprises tandem hot dog-fold thioesterase domains and a lipid-binding C-terminal steroidogenic acute regulatory protein-related lipid transfer (START) domain. To better define its role in metabolic regulation, this study examined the biochemical and enzymatic properties of Them1. Purified recombinant Them1 dimerized in solution to form an active fatty acyl-CoA thioesterase. Dimerization was induced by fatty acyl-CoAs, coenzyme A (CoASH), ATP, and ADP. Them1 hydrolyzed a range of fatty acyl-CoAs but exhibited a relative preference for long-chain molecular species. Thio</pubmed_abstract><journal>Journal of lipid research</journal><pubmed_title>Functional characterization of thioesterase superfamily member 1/Acyl-CoA thioesterase 11: implications for metabolic regulation.</pubmed_title><pmcid>PMC3494255</pmcid><funding_grant_id>R29 DK048873</funding_grant_id><funding_grant_id>P30 DK34854</funding_grant_id><funding_grant_id>DK48873</funding_grant_id><funding_grant_id>R01 DK048873</funding_grant_id><funding_grant_id>DK56626</funding_grant_id><funding_grant_id>R01 DK056626</funding_grant_id><funding_grant_id>P30 DK034854</funding_grant_id><funding_grant_id>R37 DK048873</funding_grant_id><pubmed_authors>Cohen DE</pubmed_authors><pubmed_authors>Han S</pubmed_authors></additional><is_claimable>false</is_claimable><name>Functional characterization of thioesterase superfamily member 1/Acyl-CoA thioesterase 11: implications for metabolic regulation.</name><description>Thioesterase superfamily member 1 (Them1; synonyms acyl-CoA thioesterase 11 and StarD14) is highly expressed in brown adipose tissue and limits energy expenditure in mice. Them1 is a putative fatty acyl-CoA thioesterase that comprises tandem hot dog-fold thioesterase domains and a lipid-binding C-terminal steroidogenic acute regulatory protein-related lipid transfer (START) domain. To better define its role in metabolic regulation, this study examined the biochemical and enzymatic properties of Them1. Purified recombinant Them1 dimerized in solution to form an active fatty acyl-CoA thioesterase. Dimerization was induced by fatty acyl-CoAs, coenzyme A (CoASH), ATP, and ADP. Them1 hydrolyzed a range of fatty acyl-CoAs but exhibited a relative preference for long-chain molecular species. Thio</description><dates><release>2012-01-01T00:00:00Z</release><publication>2012 Dec</publication><modification>2025-04-21T21:43:21.533Z</modification><creation>2019-03-27T01:00:14Z</creation></dates><accession>S-EPMC3494255</accession><cross_references><pubmed>22993230</pubmed><doi>10.1194/jlr.m029538</doi><doi>10.1194/jlr.M029538</doi></cross_references></HashMap>