<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Wang S</submitter><funding>NIDDK NIH HHS</funding><funding>FIC NIH HHS</funding><pagination>347-58</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2133398</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>465(2)</volume><pubmed_abstract>Glycerol-3-phosphate acyltransferase (GPAT) catalyzes the initial and rate-limiting step in glycerolipid synthesis. Several mammalian GPAT activities have been recognized, including N-ethylmaleimide (NEM)-sensitive isoforms in microsomes and mitochondria and an NEM-resistant form in mitochondrial outer membrane (GPAT1). We have now cloned a second mitochondrial isoform, GPAT2 from mouse testis. The open-reading frame encodes a protein of 798 amino acids with a calculated mass of 88.8kDa and 27% amino acid identity to GPAT1. Testis mRNA expression was 50-fold higher than in liver or brown adipose tissue, but the specific activity of NEM-sensitive GPAT in testis mitochondria was similar to that in liver. When Cos-7 cells were transiently transfected with GPAT2, NEM-sensitive GPAT activity in</pubmed_abstract><journal>Archives of biochemistry and biophysics</journal><pubmed_title>Cloning and functional characterization of a novel mitochondrial N-ethylmaleimide-sensitive glycerol-3-phosphate acyltransferase (GPAT2).</pubmed_title><pmcid>PMC2133398</pmcid><funding_grant_id>R01 DK056598</funding_grant_id><funding_grant_id>K01 DK059931</funding_grant_id><funding_grant_id>R03 TW006034</funding_grant_id><funding_grant_id>R01 DK056598-22</funding_grant_id><funding_grant_id>R56 DK056598</funding_grant_id><pubmed_authors>Wang S</pubmed_authors><pubmed_authors>Gonzalez-Baro MR</pubmed_authors><pubmed_authors>Gong N</pubmed_authors><pubmed_authors>Mashek DG</pubmed_authors><pubmed_authors>Coleman RA</pubmed_authors><pubmed_authors>Li LO</pubmed_authors><pubmed_authors>Schwerbrock NM</pubmed_authors><pubmed_authors>Lee DP</pubmed_authors><pubmed_authors>Stapleton C</pubmed_authors><pubmed_authors>Lewin TM</pubmed_authors></additional><is_claimable>false</is_claimable><name>Cloning and functional characterization of a novel mitochondrial N-ethylmaleimide-sensitive glycerol-3-phosphate acyltransferase (GPAT2).</name><description>Glycerol-3-phosphate acyltransferase (GPAT) catalyzes the initial and rate-limiting step in glycerolipid synthesis. Several mammalian GPAT activities have been recognized, including N-ethylmaleimide (NEM)-sensitive isoforms in microsomes and mitochondria and an NEM-resistant form in mitochondrial outer membrane (GPAT1). We have now cloned a second mitochondrial isoform, GPAT2 from mouse testis. The open-reading frame encodes a protein of 798 amino acids with a calculated mass of 88.8kDa and 27% amino acid identity to GPAT1. Testis mRNA expression was 50-fold higher than in liver or brown adipose tissue, but the specific activity of NEM-sensitive GPAT in testis mitochondria was similar to that in liver. When Cos-7 cells were transiently transfected with GPAT2, NEM-sensitive GPAT activity in</description><dates><release>2007-01-01T00:00:00Z</release><publication>2007 Sep</publication><modification>2025-04-05T08:52:02.831Z</modification><creation>2019-06-06T15:54:05Z</creation></dates><accession>S-EPMC2133398</accession><cross_references><pubmed>17689486</pubmed><doi>10.1016/j.abb.2007.06.033</doi></cross_references></HashMap>