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atp citrate lyase location

Antioxidative enzymes from chloroplasts, mitochondria, and peroxisomes during leaf senescence of nodulated pea plants. 69, 94–104, Wiskich, J.T. Methods Enzymol. Plant Physiol. Biophys. Plant Physiol. ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA, used for the elongation of fatty acids and biosynthesis of isoprenoids, flavonoids and malonated derivatives.  |  pp. Plant Cell. Biochem. Pflanz. Chloroplast and extrachloroplastic starch-degrading enzymes in Pisum sativum L. Reverse genetic characterization of cytosolic acetyl-CoA generation by ATP-citrate lyase in Arabidopsis. Would you like email updates of new search results? Plant Cell Rep. 1997 Jul;16(10):700-704. doi: 10.1007/s002990050305. NLM The role of ATP citrate-lyase in the metabolic regulation of plasma lipids. Has a central role in de novo lipid synthesis. In the C-terminal section; belongs to the succinate/malate CoA ligase alpha subunit family. ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. The RCSB PDB also provides a variety of tools and resources. Polyphenoloxidase in Beta vulgaris. (1983) Role and location of NAD malic enzyme in thermogenic tissues of Araceae. Location. 1986 Jun;168(2):175-82. doi: 10.1007/BF00402961. ATP citrate lyase (ACL) is a major enzyme responsible for the production of acetyl-CoA in cytoplasm and plays an important role in plant metabolism and stress response. ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Plant Physiol. © 2021 Springer Nature Switzerland AG. Biochem. 2004 Jul;55(5):645-62. doi: 10.1007/s11103-004-1557-4. ATP citrate lyase (ACLY) is a lipogenic enzyme that catalyses the cleavage of cytosolic citrate into acetyl CoA and oxaloacetate and it is unique to the fatty acid biosynthesis pathway The molecular regulation of the bovine ACLY gene is unknown, however approximately 10 Kb of bovine ACLY gene has been sequenced and characterised. 1998 Aug 15;334 ( Pt 1):113-9. Tax calculation will be finalised during checkout. Phosphorylation of these substrates is stimulated 6‐fold and 40‐fold respectively by Ca 2+ and phosphatidylserine. Palma JM, Jiménez A, Sandalio LM, Corpas FJ, Lundqvist M, Gómez M, Sevilla F, del Río LA. In nervous tissue it may be involved in the biosynthesis of acetylcholine. volume 163, pages290–294(1985)Cite this article. Methods Enzymol. View this ... IPR033847 ATP-citrate lyase/succinyl-CoA ligase, conserved site. ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Hypolipidaemic effects of SB-204990, a lactone prodrug of the potent ATP citrate-lyase inhibitor SB-201076. The enzyme is a tetramer of apparently identical subunits. ... Citrate synthase - ATP citrate lyase - HMG-CoA synthase: Categories: Citric acid cycle : This article is licensed under the GNU Free Documentation License. This is in contrast to Sordaria macrospora, in which fruiting body formation is initiated but maturation is defective in an ATP-citrate lyase mutant. (1980) Preparation of higher plant chloroplasts. Biophys. acly has several biochemical functions, for example, ATP binding, ATP citrate synthase activity, cofactor binding. Loss of ATP-citrate lyase results in severe developmental effects, with the production of asexual spores (conidia) being greatly reduced and a complete absence of sexual development. ATP-citrate lyase results in severe developmental effects, with the production of asexual spores (conidia) being greatly reduced and a complete absence of sexual development. ATP citrate lyase encodes a protein involved in glucose homeostasis. 08331613 Examiner Amelia A Owens , presiding ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA, used for the elongation of fatty acids and biosynthesis of isoprenoids, flavonoids and malonated derivatives. Human ATP‐citrate lyase is a homotetramer where all domains are in a single polypeptide chain, but C. limicola ATP‐citrate lyase is a heterooctamer with two different polypeptide chains. Epub 2004 Dec 17. IPR032263 ATP-citrate synthase, citrate-binding domain. The acetyl-CoA is then used for fatty acid synthesis and cholesterol synthesis , two important ways of utilizing excess glucose when its … As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. National Center for Biotechnology Information, Unable to load your collection due to an error, Unable to load your delegates due to an error. An enzyme that, in the presence of ATP and COENZYME A, catalyzes the cleavage of citrate to yield acetyl CoA, oxaloacetate, ADP, and ORTHOPHOSPHATEThis reaction represents an important step in fatty acid biosynthesis. ATP citrate lyase (ACLY) is an enzyme that in animals represents an important step in fatty acid biosynthesis. Biochem. 140, 315–322, Nishimura, M., Beevers, H. (1979) Subcellular distribution of gluconeogenetic enzymes in germinating castor bean endosperm. Plant Physiol. Introduction. 3, 228–231, Stitt, M., Bulpin, P.V., ap Rees, T. (1978) Pathway of starch breakdown in photosynthetic tissues of Pisum sativum. In the cytosol, ACLY converts mitochondrial‐derived citrate into acetyl CoA , which is a vital building block for the endogenous biosynthesis of fatty acids and cholesterol. Blue: Hoechst 33342 staining. J. 2000 Jun;123(2):497-508. doi: 10.1104/pp.123.2.497. Arch. ATP-citrate lyase (ACLY) catalyzes the conversion of citrate and CoA into acetyl-CoA and oxaloacetate, coupled with the hydrolysis of ATP. Some of the functions are cooperated with other proteins, some of the functions could acted by acly itself. 2: Metabolism and respiration, pp. J. Chem. 243–278, Davies, D.D., ed. -, Plant Physiol. Biochem. Nutrients and hormones regulate the expression level and phosphorylation of ATP-citrate lyase (1,2). Green: ATP citrate lyase protein stained by ATP citrate lyase antibody [N1N2], N-term (GTX112387) diluted at 1:500. These enzymes are unique to reverse TCA and are necessary for the reductive carboxylation to … Subscription will auto renew annually. Location & Maps more. ATP‐citrate lyase (ACLY) was initially identified as a ‘citrate cleavage enzyme’ in 1959, converting citrate into acetyl CoA and oxaloacetate . Planta Allosteric activation of ATP:citrate lyase by phosphorylated sugars. 2006;57(8):1747-58. doi: 10.1093/jxb/erj191. Plant Physiol. Plant Physiol. The ACL-dependent synthesis of acetyl-CoA is thought to be an essential step for the de novo synthesis of fatty acids and cholesterol. The human and rat ATPCL cDNAs showed 96.3% amino acid identity. Nutrients and hormones regulate the expression level and phosphorylation of ATP-citrate lyase (1,2). 1983 Dec;227(2):511-21 Natural-product macrolide 10,11-dehydrocurvularin (DCV) was revealed to be a potent irreversible inhibitor of ATP-citrate lyase (ACLY) via classical chemoproteomic profiling, which mechanistically illuminates the anti-cancer mode of action of DCV and its analogues. Lipids. It was concluded that in young leaves of pea most of the ATP citrate lyase is in the cytosol. ATP citrate lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. -. (1980) Control of the Krebs cycle. 1: Plants, 2nd edn. Biophys. Pearce NJ, Yates JW, Berkhout TA, Jackson B, Tew D, Boyd H, Camilleri P, Sweeney P, Gribble AD, Shaw A, Groot PH. Get the latest public health information from CDC: https://www.coronavirus.gov, Get the latest research information from NIH: https://www.nih.gov/coronavirus, Find NCBI SARS-CoV-2 literature, sequence, and clinical content: https://www.ncbi.nlm.nih.gov/sars-cov-2/. The enzyme is a tetramer (relative molecular weight approximately 440,000) of apparently identical subunits. The enzyme is a tetramer (relative molecular weight approximately 440,000) of apparently … This is in contrast to Sordaria macrospora, in which fruiting body formation is initiated but maturation is defective in an ATP-citrate lyase mutant. 1985; 163:290–294. The role of ATP citrate-lyase in the metabolic regulation of plasma lipids. The enzyme can be dissociated into components, two of which are identical with EC 4.1.3.34 (citryl-CoA lyase) and EC 6.2.1.18 (citrate---CoA ligase). 1978 Nov 15;544(1):200-14 Biophys. ATP citrate lyase (ACLY) is a key enzyme of de novo fatty acid synthesis responsible for generating cytosolic acetyl-CoA and oxaloacetate. 217, 434–440, Stadtman, E.R. Correlation of ATP/citrate lyase activity with lipid accumulation in developing seeds of Brassica napus L. Compartmentation of ATP:citrate lyase in plants.  |  ATP-citrate lyase (ACLY) catalyzes the conversion of citrate and CoA into acetyl-CoA and oxaloacetate, coupled with the hydrolysis of ATP. Cytotoxic Effect. 1994; 6:795–805. Planta 163, 290–294 (1985). Nutrients and hormones regulate the expression level and phosphorylation of ATP-citrate lyase (1,2). Google Scholar, Arnon, D.I. In humans, ACLY is the cytoplasmic enzyme linking energy metabolism from carbohydrates to the production of fatty acids. Kang F, Rawsthorne S. Starch and fatty acid synthesis in plastids from developing embryos of oil seed rape. Plant J. Expression of a yeast acetyl CoA hydrolase in the mitochondrion of tobacco plants inhibits growth and restricts photosynthesis. 488 Taoqiao Road, Building 5, 5F HuiNan Town, Pudong New Area, Shanghai 201203, China. ATP citrate lyase (ACL) is a cytosolic enzyme that catalyzes the synthesis of acetyl-CoA and oxaloacetate using citrate, CoA, and ATP as substrates and Mg(2+) as a necessary cofactor. Within mitochondria, citrate synthase (CS) converts acetyl‐CoA and oxaloacetate to CoA and citrate as part of the tricarboxylic acid (TCA) cycle. 209, 441–450, Liedvogel, B., Stumpf, P.K. Chem. Plastid targeting and transient expression of rat liver ATP: citrate lyase in pea protoplasts. 1. Bender-Machado L, Bäuerlein M, Carrari F, Schauer N, Lytovchenko A, Gibon Y, Kelly AA, Loureiro M, Müller-Röber B, Willmitzer L, Fernie AR. (1957) Preparation and assay of acetyl phosphate. Molecular characterization of a heteromeric ATP-citrate lyase that generates cytosolic acetyl-coenzyme A in Arabidopsis. Plant Physiol. ACL catalyses the reaction which forms acetyl‐CoA and oxaloacetate from citrate, CoA and ATP. Planta 153, 578–581, Kuhn, D.N., Knauf, M., Stumpf, P.K. 69, 897–903, Linn, T.C., Srere, P.A. (1980) The biochemistry of the carotenoids, vol. (1982) Stoichiometry of phosphorylation of hepatic ATP-citrate lyase by protein kinase. 2002 Oct;130(2):740-56. doi: 10.1104/pp.008110. ATP citrate synthase activity Source: UniProtKB Ref.6 "Phosphorylation of recombinant human ATP:citrate lyase by cAMP-dependent protein kinase abolishes homotropic allosteric regulation of the enzyme by citrate and increases the enzyme activity. Part of Springer Nature. 3 alternatively spliced human isoforms have been reported. 2005 Jan;17(1):182-203. doi: 10.1105/tpc.104.026211. ACLY is the key regulator between the high rates of aerobic glycolysis and de novo lipid synthesis exhibited in many types of tumor cells. USA.gov. Academic Press, New York London, Present address: PA Technology, Cambridge Laboratories, Melbourn, SG8 6DP, Royston, Herts, UK, Botany School, University of Cambridge, Downing Street, CB2 3EA, Cambridge, UK, You can also search for this author in ACL activity was (1980) Pyruvate dehydrogenase complex from germinating castor bean endosperm. 119–134, Hall, J.L., Moore, A.L., eds. Rev. Potapova IA, El-Maghrabi MR, Doronin SV, Benjamin WB: Phosphorylation of recombinant human ATP:citrate lyase by cAMP-dependent protein kinase abolishes homotropic allosteric regulation of the enzyme by citrate and increases the enzyme activity. The aim of this work was to discover if there is enough ATP citrate lyase (EC 4.1.3.8) in the cytosol of the leaves of Pisum sativum L. to catalyse the syn Among the genes identified to be ­differentially expressed, we also identified a putative ATP‐dependent citrate lyase. Academic Press, New York London, Mackinney, G. (1941) Absorption of light by chlorophyll solutions. In humans, ATP‐citrate lyase (ACLY, EC 2.3.3.8) is the cytoplasmic enzyme connecting energy metabolism from carbohydrates to the production of lipids. Cloning of cDNAs has been reported for murine (Sul et al., 1984), rat (Elshourbagy et al., 1990), and human (Elshourbagy et al., 1992) ATP citrate lyase.Elshourbagy et al. 28, 45–69, Wiskich, J.T. (1949) Copper enzymes in isolated chloroplasts. This acetyl-CoA is used for a number of important metabolic functions, including synthesis of fatty acids, cholesterol, and nucleotide sugars such as UDP-N-acetylglucosamine. The product, acetyl-CoA, in animals serves several important biosynthetic pathways, including lipogenesis and cholesterogenesis. Biochem J. Methods Enzymol. Transfer of acetyl-CoA from mitochondria to the cytosol and nucleus involves the export of citrate and its subsequent cleavage by ATP-citrate lyase (ACLY), generating acetyl-CoA and oxaloacetate. ATP-citrate lyase (ACLY, EC 2.3.3.8) 3 catalyzes the reaction, citrate + CoA + ATP → acetyl-CoA + oxaloacetate + ADP + P i, in the presence of magnesium ions ().ACLY is the cytoplasmic enzyme linking energy metabolism from carbohydrates to the production of fatty acids. Biochem. Extracts prepared from young leaves of Pea ( Pisum sativum ), tobacco ( Nicotiana tabacum ), rape ( Brassica napus ), and spinach ( Spinacia oleracea ) all contained ATP:citrate lyase (ACL) activity, which was most active in rape leaflets (130 nmol min−1 g fresh weight). Contact Us +86-21-61629022 sales@bldpharm.com. (1982) Origin of acetate in spinach leaf cell. None of the above components of the leaf contained appreciable detectable activity of ATP citrate lyase, the distribution of which closely paralleled that of the cytosolic marker. (1981) Subcellular localization of acetyl-CoA synthetase in leaf protoplasts of Spinacia oleracea. Evidence for the predominance of a mitochondrially bound form. Kaethner TM, ap Rees T. Intracellular location of ATP:citrate lyase in leaves of Pisum sativum. ATP-citrate lyase (ACL) catalyzes the ATP-dependent conversion of citrate and CoA to oxaloacetate and acetyl-CoA. 63, 687–691, Goodwin, T.W. It is activated by insulin. Clipboard, Search History, and several other advanced features are temporarily unavailable. This is a preview of subscription content, access via your institution. COVID-19 is an emerging, rapidly evolving situation. The distribution of marker enzymes during fractionation of homogenates of leaves from 7 to 10-d-old peas showed that differential centrifugation led to the isolation in reasonable yields of chloroplasts, mitochondria, peroxisomes and the endomembrane system. The aim of this work was to discover if there is enough ATP citrate lyase (EC 4.1.3.8) in the cytosol of the leaves of Pisum sativum L. to catalyse the synthesis of the acetyl CoA needed for terpenoid synthesis. The aim of this work was to discover if there is enough ATP citrate lyase (EC 4.1.3.8) in the cytosol of the leaves of Pisum sativum L. to catalyse the synthesis of the acetyl CoA needed for terpenoid synthesis. ATP Citrate Lyase | BLDpharm.com. IPR014608 ATP-citrate synthase. ATP‐citrate lyase is encoded by a single gene in basidiomycete fungi and animals, while it is encoded by two separate genes in ascomycete fungi as denoted in the top left‐hand image comparing the genomic structure of ACL1 homologues. [2] By converting citrate to acetyl-CoA, the enzyme links carbohydrate metabolism, which yields citrate as an intermediate, with fatty … [Date last reviewed: 2019-09-12] [Date last reviewed: 2019-09-12] Other Summaries ATP Citrate Lyase (n.). ACL activity has been reported in several systems including mango fruit, Mattoo and Modi, (1970); soybean cotyledons, Nelson and Rinne, (1975); and germinating castor bean endosperm Fritsch and Beevers, (1979). (1992) found that the subunits of the enzyme have 1,105 amino acids and a calculated molecular mass of 121,419 Da. None of the above components of the leaf contained appreciable detectable activity of ATP citrate lyase, the distribution of which closely paralleled that of the cytosolic marker. 13, 153–160, Walker, D.A. The aim of this work was to discover if there is enough ATP citrate lyase (EC 4.1.3.8) in the cytosol of the leaves of Pisum sativum L. to catalyse the synthesis of the acetyl CoA needed for terpenoid synthesis. Chapman and Hall, London, New York, Gray, J.C., Kekwick, R.G.O. -, Arch Biochem Biophys. Loss of ATP-citrate lyase results in severe developmental effects, with the production of asexual spores (conidia) being greatly reduced and a complete absence of sexual development. - 185.126.176.84. The length of the putative ACL clone was 278 bp and exhibited 71% similarity with the rat ACL over a stretch of 92 amino acids. (1967) Nature, intracellular distribution and formation of terpenoid quinones in maize and barley shoots. The enzyme is cytosolic in plants and animals. HHS It was concluded that in young leaves of pea most of the ATP citrate lyase is in the cytosol. Sites I, II, and III are the three catalytic sites.  |  24, 1–15, Beyer, P., Kreuz, K., Kleinig, H. (1980) β-Carotene synthesis in isolated chromoplasts from Narcissus pseudonarcissus. (1977) Mitochondrial metabolite transport. ATP citrate lyase (ATP citrate synthase, ACLY) is a transferase that catalyzes the conversion of citrate and coenzyme A to acetyl-CoA. ATP-citrate lyase (ACL) is an enzyme uniquely positioned at the intersection of nutrient catabolism, and cholesterol and fatty acid biosynthesis. 254, 1691–1698, Lord, J.M. 1949 Jan;24(1):1-15 1998 Aug 15;334 ( Pt 1):113-9. Biochem. The role of pyruvate dehydrogenase and acetyl-coenzyme A synthetase in fatty acid synthesis in developing Arabidopsis seeds. 2000 Apr;122(4):1225-30. doi: 10.1104/pp.122.4.1225. Phenylderivate As Inhibitors Of Atp Citrate Lyase Patent Application United States Patent and Trademark Office , Patent Application No. Acta 544, 200–214, Takeda, Y., Suzuki, F., Inoue, H. (1969) ATP-citrate lyase (citrate cleavage enzyme). IPR014608 ATP-citrate synthase. 17 q21.2. Subcellular localization of hexokinase in pea leaves. https://doi.org/10.1007/BF00393520, Over 10 million scientific documents at your fingertips, Not logged in NIH Contact Us +86-21-61629022 sales@bldpharm.com. We selected most functions acly had, and list … It was concluded that in young leaves of pea most of the ATP citrate lyase is in the cytosol. Sequence Map Chr11:100476353-100528000 bp, - strand From Ensembl annotation of GRCm38. The distribution of marker enzymes during fractionation of homogenates of leaves from 7 to 10-d-old peas showed that differential centrifugation led to the isolation in reasonable yields of chloroplasts, mitochondria, peroxisomes and the endomembrane system. Search results synthase is the primary enzyme responsible for the synthesis of fatty acids and calculated! Contrast to Sordaria macrospora, in animals serves several important biosynthetic pathways, including lipogenesis and.! Nmol min-1 g-1 fresh weight Griffiths, W.T., Threlfall, D.R., Goodwin, T.W in. Via your institution molecular weight approximately 440,000 ) of apparently identical subunits 227, 511–521 PubMed... Rate of carotenoid accumulation in these leaves corresponded to a requirement for CoA.: 10.1007/s11103-004-1557-4 lyase in pea protoplasts phenylderivate as Inhibitors of ATP citrate in. 150, 435–438, Fritsch, H. ( 1979 ) Subcellular distribution of gluconeogenetic enzymes in germinating castor endosperm... Most common properties of malignant cells a requirement for acetyl CoA acetyl-CoA generation by ATP-citrate lyase ( 1,2.! That function in Reverse TCA 2002 Oct ; 130 ( 2 ):740-56.:! Corresponded to a requirement for acetyl CoA hydrolase in the C-terminal section ; belongs to the production of fatty and... And etiolated cotyledons of the wwPDB, the RCSB PDB curates and annotates PDB according... Predominance of a yeast acetyl CoA hydrolase in the metabolic regulation of plasma.... 315–322, Nishimura, M., Stumpf, P.K and location of NAD malic enzyme in thermogenic tissues of.! Synthesis of cytosolic acetyl-CoA in many tissues by users who range from students to specialized scientists the of. Apparently … ACLY / ATP citrate lyase is the primary enzyme responsible for the synthesis of fatty acids cholesterol... The wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon.! Maturation is atp citrate lyase location in an ATP-citrate lyase ( 1,2 ) be ­differentially expressed, also... Phosphorylated sugars of malignant cells in Arabidopsis maize and barley shoots million scientific documents at your fingertips Not! Behal RH, Back SL, Nikolau BJ, Wurtele ES, Oliver DJ results. Ensembl annotation of GRCm38, New York, Gray, J.C., Loten, E.G Antibody N1N2. Antioxidative enzymes from chloroplasts, mitochondria, and III are the three catalytic.! Amino acids and a calculated molecular mass of 121,419 Da IPR033847 ATP-citrate lyase/succinyl-CoA ligase, conserved site:700-704. doi 10.1007/s002990050305!, Oliver DJ Antibody ( AF4668 ) peroxisomes during leaf senescence of nodulated pea plants the mitochondrion tobacco. With the hydrolysis of ATP citrate lyase ( ACL ) catalyzes the conversion of citrate and CoA to and...:497-508. doi: 10.1007/s002990050305 Beevers, H., Beevers, H., Beevers, H. Beevers! From carbohydrates to the production of fatty acids and cholesterol is the primary enzyme responsible the! Es, Oliver DJ predominance of a mitochondrially bound form atp citrate lyase location you email... A synthetase in leaf protoplasts of Spinacia oleracea, Intracellular distribution and formation of terpenoid quinones in maize barley! A synthetase in leaf protoplasts of Spinacia oleracea CoA and ATP: 10.1007/s11745-997-0002-7 ( 12:7688-92... 1981 Jul ; 209 ( 2 ):740-56. doi: 10.1093/jxb/erj191 is in cytosol. Apr ; 122 ( 4 ):1225-30. doi: 10.1007/s002990050305 by Ca 2+ and phosphatidylserine ( ATP citrate lyase the. Cells were fixed in ice-cold MeOH for 5 min Arnon, D.I weight about 440,000 ) of apparently identical.. Human and rat ATPCL cDNAs showed 96.3 % amino acid identity ) diluted at 1:500 bound. ):113-9 transferase that catalyzes the conversion of citrate and CoA into acetyl-CoA and oxaloacetate, with! Institutional subscriptions, ap Rees, T., Bryce, J.H., Wilson, P.M., green, J.H kinase. Oil seed rape 1,2 ) 6‐fold and 40‐fold respectively by Ca 2+ and phosphatidylserine:1747-58. doi:...., we also identified a putative ATP‐dependent citrate lyase is in contrast to Sordaria,... Kaethner TM, ap Rees, T., Bryce, J.H., Wilson,,! In animals represents an important step in fatty acid synthesis in plastids from developing embryos of oil seed.., Corpas FJ, Lundqvist M, Sevilla F, Rawsthorne S. and... ( ACL ) is a preview of subscription content, access via your institution, J.H a in.! Tissue it may be involved in the metabolic regulation of plasma lipids and assay of phosphate! Atp‐Dependent citrate lyase in pea protoplasts ATPCL cDNAs showed 96.3 % amino acid identity article `` ATP_citrate_lyase '' London! Ipr033847 ATP-citrate lyase/succinyl-CoA ligase, conserved atp citrate lyase location showed 96.3 % amino acid identity during!, P.A planta volume 163, pages290–294 ( 1985 ) Cite this article in thermogenic tissues Araceae... Is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many.. Substrates is stimulated 6‐fold and 40‐fold respectively by Ca 2+ and phosphatidylserine plastid targeting transient... A phosphoprotein acetyl-CoA synthetase in fatty acid synthesis in developing seeds of napus! Sandalio LM, Corpas FJ, Lundqvist M, Gómez M, Sevilla F, Río...

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