{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang S"],"funding":["NIDDK NIH HHS","FIC NIH HHS"],"pagination":["347-58"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2133398"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["465(2)"],"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"],"journal":["Archives of biochemistry and biophysics"],"pubmed_title":["Cloning and functional characterization of a novel mitochondrial N-ethylmaleimide-sensitive glycerol-3-phosphate acyltransferase (GPAT2)."],"pmcid":["PMC2133398"],"funding_grant_id":["R01 DK056598","K01 DK059931","R03 TW006034","R01 DK056598-22","R56 DK056598"],"pubmed_authors":["Wang S","Gonzalez-Baro MR","Gong N","Mashek DG","Coleman RA","Li LO","Schwerbrock NM","Lee DP","Stapleton C","Lewin TM"],"additional_accession":[]},"is_claimable":false,"name":"Cloning and functional characterization of a novel mitochondrial N-ethylmaleimide-sensitive glycerol-3-phosphate acyltransferase (GPAT2).","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","dates":{"release":"2007-01-01T00:00:00Z","publication":"2007 Sep","modification":"2025-04-05T08:52:02.831Z","creation":"2019-06-06T15:54:05Z"},"accession":"S-EPMC2133398","cross_references":{"pubmed":["17689486"],"doi":["10.1016/j.abb.2007.06.033"]}}