{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang Y"],"funding":["China Scholarship Council","Liaoning Province Rural Science and Technology Special Action Project","National Natural Science Foundation","Shenyang Science and Technology Project","International Cooperation Project of Universities in Liaoning Province"],"pagination":["3108-3121"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11048977"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["46(4)"],"pubmed_abstract":["Farnesyl pyrophosphate synthase (FPPS) catalyzes the synthesis of C15 farnesyl diphosphate (FPP) from C5 dimethylallyl diphosphate (DMAPP) and two or three C5 isopentenyl diphosphates (IPPs). FPP is an important precursor for the synthesis of isoprenoids and is involved in multiple metabolic pathways. Here, farnesyl pyrophosphate synthase from <i>Sporobolomyces pararoseus</i> NGR (SpFPPS) was isolated and expressed by the prokaryotic expression system. The <i>SpFPPS</i> full-length genomic DNA and cDNA are 1566 bp and 1053 bp, respectively. This gene encodes a 350-amino acid protein with a predicted molecular mass of 40.33 kDa and a molecular weight of 58.03 kDa (40.33 kDa + 17.7 kDa), as detected by SDS-PAGE. The function of SpFPPS was identified by induction, purification, protein concen"],"journal":["Current issues in molecular biology"],"pubmed_title":["The Property of a Key Amino Acid Determines the Function of Farnesyl Pyrophosphate Synthase in <i>Sporobolomyces pararoseus</i> NGR."],"pmcid":["PMC11048977"],"funding_grant_id":["22-319-2-13","2022030673-JH5/104","CSC202208850002","2023-01","31271818"],"pubmed_authors":["Yan J","Li Z","Li C","Zeng N","Wang D","Zhang N","An Y","Li B","Wang Y"],"additional_accession":[]},"is_claimable":false,"name":"The Property of a Key Amino Acid Determines the Function of Farnesyl Pyrophosphate Synthase in <i>Sporobolomyces pararoseus</i> NGR.","description":"Farnesyl pyrophosphate synthase (FPPS) catalyzes the synthesis of C15 farnesyl diphosphate (FPP) from C5 dimethylallyl diphosphate (DMAPP) and two or three C5 isopentenyl diphosphates (IPPs). FPP is an important precursor for the synthesis of isoprenoids and is involved in multiple metabolic pathways. Here, farnesyl pyrophosphate synthase from <i>Sporobolomyces pararoseus</i> NGR (SpFPPS) was isolated and expressed by the prokaryotic expression system. The <i>SpFPPS</i> full-length genomic DNA and cDNA are 1566 bp and 1053 bp, respectively. This gene encodes a 350-amino acid protein with a predicted molecular mass of 40.33 kDa and a molecular weight of 58.03 kDa (40.33 kDa + 17.7 kDa), as detected by SDS-PAGE. The function of SpFPPS was identified by induction, purification, protein concen","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Apr","modification":"2026-04-08T19:47:25.069Z","creation":"2026-04-08T14:30:38.902Z"},"accession":"S-EPMC11048977","cross_references":{"pubmed":["38666925"],"doi":["10.3390/cimb46040195"]}}