PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17604220-4 2007 Our previous work has shown Faa1p is a principal component of a fatty acid transport/activation complex that also includes the fatty acid transport protein Fat1p. Fatty Acids 64-74 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 28-33 26450510-4 2016 Proteins involved in glycolysis, acetate metabolism, fatty acid synthesis, TCA cycle, glyoxylate cycle, the pentose phosphate pathway, respiration, transportation, and stress response were found to be upregulated in faa1 faa4 [Acot5s] as compared to the wild type. Fatty Acids 53-63 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 217-226 26450510-6 2016 Taken together with our metabolite analysis, our results showed that the disruption of Faa1 and Faa4 and expression of Acot5s in the engineered strain faa1 faa4 [Acot5s] not only relieved the feedback inhibition of fatty acyl-CoAs on fatty acid synthesis, but also caused a major metabolic rearrangement. Fatty Acids 235-245 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 87-91 26450510-6 2016 Taken together with our metabolite analysis, our results showed that the disruption of Faa1 and Faa4 and expression of Acot5s in the engineered strain faa1 faa4 [Acot5s] not only relieved the feedback inhibition of fatty acyl-CoAs on fatty acid synthesis, but also caused a major metabolic rearrangement. Fatty Acids 235-245 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 152-161 24769906-7 2014 The extracellular total fatty acids (TFA) in the strain faa1 faa4 [Acot5s] increased to 6.43-fold as compared to the wild-type strain during the stationary phase. Fatty Acids 24-35 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 57-66 17679730-1 2007 The fatty acid transport protein (FATP) Fat1p in the yeast Saccharomyces cerevisiae functions in concert with acyl-coenzyme A synthetase (ACSL; either Faa1p or Faa4p) in vectorial acylation, which couples the transport of exogenous fatty acids with activation to CoA thioesters. Fatty Acids 4-14 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 151-156 17679730-1 2007 The fatty acid transport protein (FATP) Fat1p in the yeast Saccharomyces cerevisiae functions in concert with acyl-coenzyme A synthetase (ACSL; either Faa1p or Faa4p) in vectorial acylation, which couples the transport of exogenous fatty acids with activation to CoA thioesters. Fatty Acids 232-243 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 151-156 17679730-10 2007 This topological orientation is consistent with the mechanistic roles of both Fat1p and Faa1p or Faa4p in the coupled transport/activation of exogenous fatty acids by vectorial acylation. Fatty Acids 152-163 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 88-93 28298234-2 2017 Deletion of the fatty acyl-CoA synthetase genes FAA1 and FAA4 is an effective and straightforward way to disable re-activation of fatty acids and drastically increase FFA levels. Fatty Acids 130-141 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 48-52 17604220-4 2007 Our previous work has shown Faa1p is a principal component of a fatty acid transport/activation complex that also includes the fatty acid transport protein Fat1p. Fatty Acids 127-137 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 28-33 17604220-6 2007 In order to further define the role of this enzyme in fatty acid transport-coupled activation (vectorial acylation), initial velocity kinetic studies were completed to define the kinetic parameters of Faa1p in response to the different substrates and to define mechanism. Fatty Acids 54-64 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 201-206 16233436-4 2003 The mutation that causes the fatty acid secretion phenotype occurred at a single allele, and this phenotype was suppressed by the introduction of a single copy of FAA1, a gene for acyl-CoA Synthetase, to the mutant. Fatty Acids 29-39 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 163-167 16798075-5 2007 Pivotal roles have been defined for Faa1p and Faa4p in fatty acid import, beta-oxidation and transcriptional control mediated by the transcription factors Oaf1p/Pip2p and Mga2p/Spt23p. Fatty Acids 55-65 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 36-41 12601005-14 2003 Collectively, these data support the hypothesis that fatty acid import by vectorial acylation in yeast requires a multiprotein complex, which consists of Fat1p and Faa1p or Faa4p. Fatty Acids 53-63 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 164-169 16233436-5 2003 Although the mutation expressing this phenotype was not within FAA1 in YTS51, the disruption of FAA1 in the wild-type strain resulted in fatty acid secretion even though the level of fatty acid secretion was less than that in YTS51. Fatty Acids 137-147 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 96-100 16233436-5 2003 Although the mutation expressing this phenotype was not within FAA1 in YTS51, the disruption of FAA1 in the wild-type strain resulted in fatty acid secretion even though the level of fatty acid secretion was less than that in YTS51. Fatty Acids 183-193 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 96-100 11477098-0 2001 The Acyl-CoA synthetases encoded within FAA1 and FAA4 in Saccharomyces cerevisiae function as components of the fatty acid transport system linking import, activation, and intracellular Utilization. Fatty Acids 112-122 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 40-44 11477098-3 2001 Faa1p or Faa4p are essential for long-chain fatty acid import, suggesting that one or both of these enzymes are components of the fatty acid transport system, which also includes Fat1p. Fatty Acids 44-54 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 0-5 11477098-11 2001 Northern analyses demonstrated an additional defect in fatty acid trafficking as FAA1 or FAA4 were required for the transcriptional regulation of the genes encoding the peroxisomal enzymes acyl-CoA oxidase (POX1) and medium-chain acyl-CoA synthetase (FAA2). Fatty Acids 55-65 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 81-85 11477098-12 2001 These data support the hypothesis that fatty acyl-CoA synthetase (Faa1p or Faa4p) functions as a component of the fatty acid import system by linking import and activation of exogenous fatty acids to intracellular utilization and signaling. Fatty Acids 114-124 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 66-71 11477098-12 2001 These data support the hypothesis that fatty acyl-CoA synthetase (Faa1p or Faa4p) functions as a component of the fatty acid import system by linking import and activation of exogenous fatty acids to intracellular utilization and signaling. Fatty Acids 185-196 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 66-71 7738025-4 1995 The functionally interchangeable FAA1 and FAA4 genes are responsible for activation of these imported fatty acids. Fatty Acids 102-113 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 33-37 16232807-1 2000 Fatty acid activation gene (FAA1) in sake yeast Kyokai no. Fatty Acids 0-10 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 28-32 9675816-9 1998 As has been reported for OLE1, the repression of ATF1 by unsaturated fatty acids was relieved in a disruptant carrying a faa1 and faa4 double mutation, two fatty acid activation genes. Fatty Acids 69-79 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 121-125 8631965-10 1996 Two fatty acid activation genes, FAA1 and FAA4, were found to be essential for unsaturated fatty acid repression of OLE1 through the FAR sequences. Fatty Acids 4-14 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 33-37 7650027-3 1995 Recent genetic studies indicate that Faa1p and Faa4p are involved in the activation of imported fatty acids, while Faa2p activates endogenous pools of fatty acids. Fatty Acids 96-107 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 37-42 9748261-2 1998 Faa1p and Faa4p activate exogenously derived fatty acids. Fatty Acids 45-56 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 0-5 8206942-5 1994 In vitro assays of C3:0-C24:0 fatty acids indicate that Faa1p prefers C12:0-C16:0, with myristic and pentadecanoic acid (C15:0) having the highest activities. Fatty Acids 30-41 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 56-61 8027063-4 1994 We have isolated and characterized three unlinked Fatty Acid Activation genes from S. cerevisiae, FAA1, FAA2, and FAA3. Fatty Acids 50-60 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 98-102 1572893-3 1992 The FAA1 (fatty acid activation) gene has been isolated by genetic complementation of a faal mutant. Fatty Acids 10-20 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 4-8 8440712-11 1993 Faa1p can also rescue growth at 37 degrees C of fadD- strains on minimal media supplemented with C12:0, although this rescue becomes less efficient as the chain length of the supplemental fatty acid increases. Fatty Acids 188-198 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 0-5 26019148-4 2015 However, FAT2-FAT4 deletion mutants did not show any growth defects, suggesting that FAT1 and FAA1 are involved in the activation of fatty acids produced during the metabolism of n-alkanes. Fatty Acids 133-144 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 94-98 26019148-7 2015 However, the FAA1 deletion mutant did not grow, indicating a critical role for FAA1 in the utilization of fatty acids. Fatty Acids 106-117 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 13-17 26019148-7 2015 However, the FAA1 deletion mutant did not grow, indicating a critical role for FAA1 in the utilization of fatty acids. Fatty Acids 106-117 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 79-83 18422644-3 2008 The combined deletion of Faa1p and Faa4p encoding two out of five acyl-CoA synthetases was necessary and sufficient to establish mutant cells that secreted fatty acids in a growth-phase dependent manner. Fatty Acids 156-167 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 25-30 18422644-9 2008 Therefore, we propose the recycling of endogenous fatty acids generated in the course of lipid remodelling as a major task of both acyl-CoA synthetases Faa1p and Faa4p. Fatty Acids 50-61 long-chain fatty acid-CoA ligase FAA1 Saccharomyces cerevisiae S288C 152-157