PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 31376476-1 2019 Malonyl-CoA synthetase (ACSF3) catalyzes the first step of the mitochondrial fatty acid biosynthesis (mtFASII). Fatty Acids 77-87 acyl-CoA synthetase family member 3 Homo sapiens 0-22 31376476-1 2019 Malonyl-CoA synthetase (ACSF3) catalyzes the first step of the mitochondrial fatty acid biosynthesis (mtFASII). Fatty Acids 77-87 acyl-CoA synthetase family member 3 Homo sapiens 24-29 26915364-1 2016 BACKGROUND: The presence of increased urinary concentrations of both methylmalonic acid (MMA) and malonic acid (MA) is assumed to differentiate combined malonic and methylmalonic aciduria (CMAMMA), due to mutations in the ACSF3 gene, from other causes of methylmalonic aciduria (classic MMAemia). Methylmalonic Acid 69-87 acyl-CoA synthetase family member 3 Homo sapiens 222-227 30201289-3 2019 While these canonical cytoplasmic roles of malonyl-CoA have been well described, malonyl-CoA can also be generated within the mitochondrial matrix by an alternative pathway: the ATP-dependent ligation of malonate to Coenzyme A by the malonyl-CoA synthetase ACSF3. Malonyl Coenzyme A 81-92 acyl-CoA synthetase family member 3 Homo sapiens 234-256 30201289-3 2019 While these canonical cytoplasmic roles of malonyl-CoA have been well described, malonyl-CoA can also be generated within the mitochondrial matrix by an alternative pathway: the ATP-dependent ligation of malonate to Coenzyme A by the malonyl-CoA synthetase ACSF3. Malonyl Coenzyme A 81-92 acyl-CoA synthetase family member 3 Homo sapiens 257-262 30201289-3 2019 While these canonical cytoplasmic roles of malonyl-CoA have been well described, malonyl-CoA can also be generated within the mitochondrial matrix by an alternative pathway: the ATP-dependent ligation of malonate to Coenzyme A by the malonyl-CoA synthetase ACSF3. Adenosine Triphosphate 178-181 acyl-CoA synthetase family member 3 Homo sapiens 234-256 30201289-3 2019 While these canonical cytoplasmic roles of malonyl-CoA have been well described, malonyl-CoA can also be generated within the mitochondrial matrix by an alternative pathway: the ATP-dependent ligation of malonate to Coenzyme A by the malonyl-CoA synthetase ACSF3. Adenosine Triphosphate 178-181 acyl-CoA synthetase family member 3 Homo sapiens 257-262 30201289-3 2019 While these canonical cytoplasmic roles of malonyl-CoA have been well described, malonyl-CoA can also be generated within the mitochondrial matrix by an alternative pathway: the ATP-dependent ligation of malonate to Coenzyme A by the malonyl-CoA synthetase ACSF3. malonic acid 204-212 acyl-CoA synthetase family member 3 Homo sapiens 234-256 30201289-3 2019 While these canonical cytoplasmic roles of malonyl-CoA have been well described, malonyl-CoA can also be generated within the mitochondrial matrix by an alternative pathway: the ATP-dependent ligation of malonate to Coenzyme A by the malonyl-CoA synthetase ACSF3. malonic acid 204-212 acyl-CoA synthetase family member 3 Homo sapiens 257-262 30201289-5 2019 A major role for ACSF3 is to provide a metabolic pathway for the clearance of malonate by the generation of malonyl-CoA, which can then be decarboxylated to acetyl-CoA by malonyl-CoA decarboxylase. malonic acid 78-86 acyl-CoA synthetase family member 3 Homo sapiens 17-22 30201289-5 2019 A major role for ACSF3 is to provide a metabolic pathway for the clearance of malonate by the generation of malonyl-CoA, which can then be decarboxylated to acetyl-CoA by malonyl-CoA decarboxylase. Malonyl Coenzyme A 108-119 acyl-CoA synthetase family member 3 Homo sapiens 17-22 30201289-5 2019 A major role for ACSF3 is to provide a metabolic pathway for the clearance of malonate by the generation of malonyl-CoA, which can then be decarboxylated to acetyl-CoA by malonyl-CoA decarboxylase. Acetyl Coenzyme A 157-167 acyl-CoA synthetase family member 3 Homo sapiens 17-22 30201289-6 2019 Additionally, ACSF3-derived malonyl-CoA can be used to malonylate lysine residues on proteins within the matrix of mitochondria, possibly adding another regulatory layer to post-translational control of mitochondrial metabolism. Malonyl Coenzyme A 28-39 acyl-CoA synthetase family member 3 Homo sapiens 14-19 30201289-6 2019 Additionally, ACSF3-derived malonyl-CoA can be used to malonylate lysine residues on proteins within the matrix of mitochondria, possibly adding another regulatory layer to post-translational control of mitochondrial metabolism. Lysine 66-72 acyl-CoA synthetase family member 3 Homo sapiens 14-19 30201289-7 2019 The discovery of ACSF3-mediated generation of malonyl-CoA defines a new mitochondrial metabolic pathway and raises new questions about how the metabolic fates of this multifunctional metabolite intersect with mitochondrial metabolism. Malonyl Coenzyme A 46-57 acyl-CoA synthetase family member 3 Homo sapiens 17-22 28986507-0 2017 A conserved mammalian mitochondrial isoform of acetyl-CoA carboxylase ACC1 provides the malonyl-CoA essential for mitochondrial biogenesis in tandem with ACSF3. Malonyl Coenzyme A 88-99 acyl-CoA synthetase family member 3 Homo sapiens 154-159 28479296-2 2017 Intramitochondrial malonyl-CoA is generated by a malonyl-CoA synthetase, ACSF3, which produces malonyl-CoA from malonate, an endogenous competitive inhibitor of succinate dehydrogenase. Malonyl Coenzyme A 19-30 acyl-CoA synthetase family member 3 Homo sapiens 73-78 28479296-2 2017 Intramitochondrial malonyl-CoA is generated by a malonyl-CoA synthetase, ACSF3, which produces malonyl-CoA from malonate, an endogenous competitive inhibitor of succinate dehydrogenase. Malonyl Coenzyme A 49-60 acyl-CoA synthetase family member 3 Homo sapiens 73-78 28479296-2 2017 Intramitochondrial malonyl-CoA is generated by a malonyl-CoA synthetase, ACSF3, which produces malonyl-CoA from malonate, an endogenous competitive inhibitor of succinate dehydrogenase. malonic acid 112-120 acyl-CoA synthetase family member 3 Homo sapiens 73-78 28479296-4 2017 ACSF3 KO cells exhibited elevated malonate and impaired mitochondrial metabolism. malonic acid 34-42 acyl-CoA synthetase family member 3 Homo sapiens 0-5 28479296-6 2017 While ACSF3 was required for the metabolism and therefore detoxification of malonate, ACSF3-derived malonyl-CoA was specifically required for lysine malonylation of mitochondrial proteins. malonic acid 76-84 acyl-CoA synthetase family member 3 Homo sapiens 6-11 28479296-6 2017 While ACSF3 was required for the metabolism and therefore detoxification of malonate, ACSF3-derived malonyl-CoA was specifically required for lysine malonylation of mitochondrial proteins. Malonyl Coenzyme A 100-111 acyl-CoA synthetase family member 3 Homo sapiens 86-91 28479296-6 2017 While ACSF3 was required for the metabolism and therefore detoxification of malonate, ACSF3-derived malonyl-CoA was specifically required for lysine malonylation of mitochondrial proteins. Lysine 142-148 acyl-CoA synthetase family member 3 Homo sapiens 86-91 28479296-7 2017 Together, these data describe an essential role for ACSF3 in dictating the metabolic fate of mitochondrial malonate and malonyl-CoA in mammalian metabolism. malonic acid 107-115 acyl-CoA synthetase family member 3 Homo sapiens 52-57 28479296-7 2017 Together, these data describe an essential role for ACSF3 in dictating the metabolic fate of mitochondrial malonate and malonyl-CoA in mammalian metabolism. Malonyl Coenzyme A 120-131 acyl-CoA synthetase family member 3 Homo sapiens 52-57 28644952-1 2017 In this issue of Cell Chemical Biology, Bowman and colleagues show that the mitochondrial enzyme ACSF3 generates malonyl-CoA from malonate, in turn regulating metabolic flux and mitochondrial protein malonylation (Bowman et al., 2017). Malonyl Coenzyme A 113-124 acyl-CoA synthetase family member 3 Homo sapiens 97-102 28644952-1 2017 In this issue of Cell Chemical Biology, Bowman and colleagues show that the mitochondrial enzyme ACSF3 generates malonyl-CoA from malonate, in turn regulating metabolic flux and mitochondrial protein malonylation (Bowman et al., 2017). malonic acid 130-138 acyl-CoA synthetase family member 3 Homo sapiens 97-102 26915364-1 2016 BACKGROUND: The presence of increased urinary concentrations of both methylmalonic acid (MMA) and malonic acid (MA) is assumed to differentiate combined malonic and methylmalonic aciduria (CMAMMA), due to mutations in the ACSF3 gene, from other causes of methylmalonic aciduria (classic MMAemia). Methylmalonic Acid 89-92 acyl-CoA synthetase family member 3 Homo sapiens 222-227 26915364-1 2016 BACKGROUND: The presence of increased urinary concentrations of both methylmalonic acid (MMA) and malonic acid (MA) is assumed to differentiate combined malonic and methylmalonic aciduria (CMAMMA), due to mutations in the ACSF3 gene, from other causes of methylmalonic aciduria (classic MMAemia). malonic acid 75-87 acyl-CoA synthetase family member 3 Homo sapiens 222-227 24108359-1 2013 The trisubstituted enolate- and C-C bond-forming capacities of engineered carboxymethylproline synthases CMPSs are coupled with the malonyl-CoA synthetase MatB to enable stereoselective preparation of 5- and 6-membered N-heterocycles functionalised with alkyl-substituted carboxymethyl side chains, starting from achiral alkyl-substituted malonic acids and L-amino acid semialdehydes. Nitrogen 219-220 acyl-CoA synthetase family member 3 Homo sapiens 132-154 24108359-1 2013 The trisubstituted enolate- and C-C bond-forming capacities of engineered carboxymethylproline synthases CMPSs are coupled with the malonyl-CoA synthetase MatB to enable stereoselective preparation of 5- and 6-membered N-heterocycles functionalised with alkyl-substituted carboxymethyl side chains, starting from achiral alkyl-substituted malonic acids and L-amino acid semialdehydes. alkyl-substituted carboxymethyl 254-285 acyl-CoA synthetase family member 3 Homo sapiens 132-154 24108359-1 2013 The trisubstituted enolate- and C-C bond-forming capacities of engineered carboxymethylproline synthases CMPSs are coupled with the malonyl-CoA synthetase MatB to enable stereoselective preparation of 5- and 6-membered N-heterocycles functionalised with alkyl-substituted carboxymethyl side chains, starting from achiral alkyl-substituted malonic acids and L-amino acid semialdehydes. alkyl-substituted malonic acids 321-352 acyl-CoA synthetase family member 3 Homo sapiens 132-154 24108359-1 2013 The trisubstituted enolate- and C-C bond-forming capacities of engineered carboxymethylproline synthases CMPSs are coupled with the malonyl-CoA synthetase MatB to enable stereoselective preparation of 5- and 6-membered N-heterocycles functionalised with alkyl-substituted carboxymethyl side chains, starting from achiral alkyl-substituted malonic acids and L-amino acid semialdehydes. l-amino acid semialdehydes 357-383 acyl-CoA synthetase family member 3 Homo sapiens 132-154 21846720-0 2011 Mammalian ACSF3 protein is a malonyl-CoA synthetase that supplies the chain extender units for mitochondrial fatty acid synthesis. Fatty Acids 109-119 acyl-CoA synthetase family member 3 Homo sapiens 10-15 23337955-9 2013 ACSF3 was significantly upregulated, and was involved in fatty acid and lipid metabolism and accelerated liver injury. Fatty Acids 69-79 acyl-CoA synthetase family member 3 Homo sapiens 0-5 21846720-4 2011 The human candidate protein ACSF3, which has a predicted N-terminal mitochondrial targeting sequence, was cloned, expressed, and characterized as a 65-kDa acyl-CoA synthetase with extremely high specificity for malonate and methylmalonate. malonic acid 211-219 acyl-CoA synthetase family member 3 Homo sapiens 28-33 21846720-5 2011 An arginine residue implicated in malonate binding by prokaryotic malonyl-CoA synthetases was found to be positionally conserved in animal ACSF3 enzymes and essential for activity. Arginine 3-11 acyl-CoA synthetase family member 3 Homo sapiens 139-144 21846720-5 2011 An arginine residue implicated in malonate binding by prokaryotic malonyl-CoA synthetases was found to be positionally conserved in animal ACSF3 enzymes and essential for activity. malonic acid 34-42 acyl-CoA synthetase family member 3 Homo sapiens 139-144 21846720-7 2011 In conclusion, unlike fungi, which have an intramitochondrial acetyl-CoA carboxylase, animals require an alternative source of mitochondrial malonyl-CoA; the mitochondrial ACSF3 enzyme is capable of filling this role by utilizing free malonic acid as substrate. malonic acid 235-247 acyl-CoA synthetase family member 3 Homo sapiens 172-177 19653678-2 2009 Malonyl-CoA synthetase (MCS) was used in conjunction with chalcone synthase (CHS), thereby allowing efficient use of synthetic starter molecules and malonate as extender. malonic acid 149-157 acyl-CoA synthetase family member 3 Homo sapiens 0-22 11403625-0 2001 Remarkably broad substrate tolerance of malonyl-CoA synthetase, an enzyme capable of intracellular synthesis of polyketide precursors. Polyketides 112-122 acyl-CoA synthetase family member 3 Homo sapiens 40-62 35221709-4 2022 Acyl-CoA synthetase family member 3 (ACSF3) encodes malonyl-CoA synthetase that is involved in the synthesis and oxidation of fatty acids. Fatty Acids 126-137 acyl-CoA synthetase family member 3 Homo sapiens 0-35 35221709-4 2022 Acyl-CoA synthetase family member 3 (ACSF3) encodes malonyl-CoA synthetase that is involved in the synthesis and oxidation of fatty acids. Fatty Acids 126-137 acyl-CoA synthetase family member 3 Homo sapiens 37-42 35221709-4 2022 Acyl-CoA synthetase family member 3 (ACSF3) encodes malonyl-CoA synthetase that is involved in the synthesis and oxidation of fatty acids. Fatty Acids 126-137 acyl-CoA synthetase family member 3 Homo sapiens 52-74 35071379-3 2021 In this research, we verified the relationship between expression of the ACSF3 and the production of triglycerides (TGs) at the cellular level by silencing and over-expressing ACSF3. Triglycerides 101-114 acyl-CoA synthetase family member 3 Homo sapiens 73-78 35071379-3 2021 In this research, we verified the relationship between expression of the ACSF3 and the production of triglycerides (TGs) at the cellular level by silencing and over-expressing ACSF3. Triglycerides 101-114 acyl-CoA synthetase family member 3 Homo sapiens 176-181 35071379-3 2021 In this research, we verified the relationship between expression of the ACSF3 and the production of triglycerides (TGs) at the cellular level by silencing and over-expressing ACSF3. Triglycerides 116-119 acyl-CoA synthetase family member 3 Homo sapiens 73-78 35071379-3 2021 In this research, we verified the relationship between expression of the ACSF3 and the production of triglycerides (TGs) at the cellular level by silencing and over-expressing ACSF3. Triglycerides 116-119 acyl-CoA synthetase family member 3 Homo sapiens 176-181