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ATP citrate synthase

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758:(CCL) found in deep branching bacteria. This CCL module catalyses the cleavage of the citryl-CoA intermediate into the products acetyl-CoA and oxaloacetate. In 2019, cryo-EM structures of human ACLY, alone or bound to substrates or products were reported as well. ACLY forms a homotetramer with a rigid citrate synthase homology (CSH) module, flanked by four flexible acetyl-CoA synthetase homology (ASH) domains; CoA is bound at the CSH–ASH interface in mutually exclusive productive or unproductive conformations. The structure of a catalytic mutant of ACLY in the presence of ATP, citrate and CoA substrates reveals a CoA and phosphor-citrate intermediate in the N-terminal domain. Cryo-EM structures of products bound ACLY and substrates bound ACLY were also determined at 3.0 Å and 3.1 Å. An EM structure of mutant E599Q in complex with CoA and phospho-citrate intermediate was determined at resolution of 2.9 Å. Comparison between these structures of apo-ACLY and ligands bound ACLY demonstrated conformational changes on ASH domain (N-terminal domain) when different ligands bind. 1545: 732:. In 2019, a full length structure of human ACLY in complex with the substrates coenzyme A, citrate and Mg.ADP was determined by X-ray crystallography to a resolution of 3.2 Å. Moreover, in 2019 a full length structure of ACLY in complex with an inhibitor was determined by cryo-EM methods to a resolution of 3.7 Å. Additional structures of heteromeric ACLY-A/B from the 241: 754:. Full length ACLY structures showed that the tetrameric protein oligomerizes via its C-terminal domain. The C-terminal domain had not been observed in the previously determined truncated crystal structures. The C-terminal region of ACLY assembles in a tetrameric module that is structurally similar to 497:
In plants, ATP citrate lyase generates acetyl-CoA for cytosolically-synthesized metabolites; Acetyl-CoA is not transported across subcellular membranes of plants. Such metabolites include: elongated fatty acids (used in seed oils, membrane
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3MWE, 3PFF, 5TDE, 5TDF, 5TDM, 5TDZ, 5TE1, 5TEQ, 5TES, 5TET, 6HXH, 6HXK, 6HXL, 6HXM, 6O0H, 6QFB 3MWD, 3MWE, 3PFF, 5TDE, 5TDF, 5TDM, 5TDZ, 5TE1, 5TEQ, 5TES, 5TET, 6HXH, 6HXK, 6HXL, 6HXM, 6O0H, 6QFB
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Aoshima M, Ishii M, Igarashi Y (May 2004). "A novel enzyme, citryl-CoA lyase, catalysing the second step of the citrate cleavage reaction in Hydrogenobacter thermophilus TK-6".
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Lovell SC, Davis IW, Arendall WB, de Bakker PI, Word JM, Prisant MG, et al. (February 2003). "Structure validation by Calpha geometry: phi,psi and Cbeta deviation".
562:); malonyl and acyl-derivatives (d-amino acids, malonylated flavonoids, acylated, prenylated and malonated proteins). De novo fatty acid biosynthesis in plants occurs in 195: 272: 214: 1776: 1771: 1165:
Wei J, Leit S, Kuai J, Therrien E, Rafi S, Harwood HJ, et al. (April 2019). "An allosteric mechanism for potent inhibition of human ATP-citrate lyase".
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Lill U, Schreil A, Eggerer H (July 1982). "Isolation of enzymically active fragments formed by limited proteolysis of ATP citrate lyase".
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of apparently identical subunits. In animals, the product, acetyl-CoA, is used in several important biosynthetic pathways, including
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Ray KK, Bays HE, Catapano AL, Lalwani ND, Bloedon LT, Sterling LR, et al. (CLEAR Harmony Trial) (March 2019).
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Srere PA, Lipmann F (1953). "An enzymatic reaction between citrate, adenosine triphosphate and coenzyme A".
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citrate synthase domain. The cleft between the CoA binding and citrate synthase domains forms the
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Verschueren KH, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, et al. (April 2019).
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Crystal structure of human ATP citrate lyase in complex with citrate, coenzyme A and Mg.ADP.
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Elshourbagy NA, Near JC, Kmetz PJ, Wells TN, Groot PH, Saxty BA, et al. (March 1992).
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Fatland BL, Ke J, Anderson MD, Mentzen WI, Cui LW, Allred CC, et al. (October 2002).
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In 2010, a structure of truncated human ATP citrate lyase was determined using
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ATP citrate lyase is responsible for catalyzing the conversion of citrate and
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genes probably occurred early in the evolutionary history of this kingdom.
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Pietrocola F, Galluzzi L, Bravo-San Pedro JM, Madeo F, Kroemer G (2015).
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ATP citrate lyase is the primary enzyme responsible for the synthesis of
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Wei X, Schultz K, Bazilevsky GA, Vogt A, Marmorstein R (January 2020).
742: 713:, followed by a CoA binding domain and CoA-ligase domain and finally a 666: 630: 587: 563: 519: 448: 428: 313: 122: 103: 980: 2475: 2470: 2278: 2198: 1968: 1899: 1727: 1722: 1663: 547: 460: 420: 320: 202: 98: 86: 74: 766:
The enzyme's action can be inhibited by the coenzyme A-conjugate of
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Wei X, Schultz K, Bazilevsky GA, Vogt A, Marmorstein R (May 2020).
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Guay C, Madiraju SR, Aumais A, Joly E, Prentki M (December 2007).
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of the enzyme, where both citrate and acetyl-coenzyme A bind.
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citrate + ATP + CoA → oxaloacetate + Acetyl-CoA + ADP + P
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Sun T, Hayakawa K, Bateman KS, Fraser ME (August 2010).
1085:"ATP-Citrate Lyase: A Key Player in Cancer Metabolism" 1533: 2598: 2579: 2559: 2541: 2518: 2444: 2435: 2407: 2398: 2373: 2354: 2316: 2292: 2285: 2124: 2088: 2057: 2026: 1975: 1839: 1790: 1602: 396: 386: 381: 360: 348: 343: 331: 319: 307: 295: 283: 271: 263: 255: 250: 233: 213: 201: 189: 184: 164: 145: 133: 121: 109: 97: 85: 73: 68: 56: 44: 39: 34: 451:acetyl-CoA precursors of thousands of specialized 423:that in animals represents an important step in 778:in February 2020 for use in the United States. 958: 956: 954: 952: 2244: 1953: 1571: 8: 1777:2-acylglycerol-3-phosphate O-acyltransferase 1772:1-acylglycerol-3-phosphate O-acyltransferase 2441: 2404: 2289: 2251: 2237: 2229: 1960: 1946: 1938: 1578: 1564: 1556: 1524:United States National Library of Medicine 641:The enzyme is composed of two subunits in 378: 239: 181: 1513:at the U.S. National Library of Medicine 1386: 1376: 1335: 1325: 1314:Nature Structural & Molecular Biology 1284: 1265:Nature Structural & Molecular Biology 1141: 1100: 1069:at the U.S. National Library of Medicine 1043: 988: 932: 922: 876: 1522:This article incorporates text from the 1485:Journal of the American Chemical Society 774:in humans. The drug was approved by the 1540: 786: 1767:Glycerol-3-phosphate O-acyltransferase 750:show that the architecture of ACLY is 705:The mammalian ATP citrate lyase has a 230: 31: 1760:Lecithin—cholesterol acyltransferase 1083:Zaidi N, Swinnen JV, Smans K (2012). 709:citrate-binding domain that adopts a 7: 2567:Hydroxyacyl-Coenzyme A dehydrogenase 1755:Glyceronephosphate O-acyltransferase 900: 898: 896: 796: 794: 792: 790: 690:Animal ACL enzymes are homomeric; a 2422:Carnitine-acylcarnitine translocase 1927:Sulfoacetaldehyde acetyltransferase 1619:Acetyl-Coenzyme A acetyltransferase 1365:The New England Journal of Medicine 1032:The Journal of Biological Chemistry 911:The Journal of Biological Chemistry 617:This enzyme was formerly given the 2381:Glycerol-3-phosphate dehydrogenase 1843:: converted into alkyl on transfer 1468:10.1111/j.1432-1033.1982.tb06731.x 878:10.1111/j.1432-1033.1992.tb16659.x 25: 2608:Long-chain-aldehyde dehydrogenase 2427:Carnitine palmitoyltransferase II 1649:Chloramphenicol acetyltransferase 482:in many tissues. The enzyme is a 2417:Carnitine palmitoyltransferase I 1701:Carnitine O-palmitoyltransferase 1543: 1456:European Journal of Biochemistry 1230:10.1111/j.1365-2958.2004.04010.x 1013:"Entrez Gene: ATP citrate lyase" 865:European Journal of Biochemistry 1644:Beta-galactoside transacetylase 1659:Serotonin N-acetyl transferase 1606:: other than amino-acyl groups 494:. It is activated by insulin. 1: 1824:Keratinocyte transglutaminase 1804:Gamma-glutamyl transpeptidase 1718:Serine C-palmitoyltransferase 1102:10.1158/0008-5472.CAN-11-4112 439:, which yields citrate as an 2633:Genes on human chromosome 17 2510:Acetyl-CoA C-acyltransferase 1745:Aminolevulinic acid synthase 1639:Acetyl-CoA C-acyltransferase 1634:Dihydrolipoyl transacetylase 776:Food and Drug Administration 2341:3-Hydroxyacyl ACP dehydrase 1907:2-hydroxyglutarate synthase 2659: 2331:Beta-ketoacyl-ACP synthase 1917:2-isopropylmalate synthase 1750:Beta-ketoacyl-ACP synthase 1624:N-Acetylglutamate synthase 1143:10.1016/j.cmet.2015.05.014 770:, a compound which lowers 582:, driven by hydrolysis of 550:; and, mevalonate-derived 2590:Malonyl-CoA decarboxylase 2551:Propionyl-CoA carboxylase 2533:2,4 Dienoyl-CoA reductase 2365:Stearoyl-CoA desaturase-1 2116:Michaelis–Menten kinetics 1865:Decylhomocitrate synthase 1676:Histone acetyltransferase 1629:Choline acetyltransferase 1327:10.1038/s41594-020-0421-9 1277:10.1038/s41594-019-0351-6 1187:10.1038/s41586-019-1094-6 830:10.1038/s41586-019-1095-5 377: 238: 180: 2336:Î’-Ketoacyl ACP reductase 2008:Diffusion-limited enzyme 1870:2-methylcitrate synthase 1515:Medical Subject Headings 1071:Medical Subject Headings 752:evolutionarily conserved 728:to a resolution of 2.10 578:(CoA) to acetyl-CoA and 417:ATP citrate lyase (ACLY) 1912:3-propylmalate synthase 1819:Tissue transglutaminase 924:10.1074/jbc.M109.078667 633:in plants and animals. 445:fatty acid biosynthesis 437:carbohydrate metabolism 425:fatty acid biosynthesis 234:Human ATP citrate lyase 2452:Acyl CoA dehydrogenase 2308:Acetyl-CoA carboxylase 1880:3-ethylmalate synthase 1875:2-ethylmalate synthase 1740:Acyltransferase like 2 1218:Molecular Microbiology 1045:10.1074/jbc.M707294200 2268:fatty acid metabolism 2101:Eadie–Hofstee diagram 2034:Allosteric regulation 1860:Citrate (Re)-synthase 1855:Decylcitrate synthase 1796:Aminoacyltransferases 1696:palmitoyltransferases 1378:10.1056/NEJMoa1803917 747:Methanosaeta concilii 734:green sulfur bacteria 596:adenosine diphosphate 590:to yield acetyl CoA, 2318:Fatty acid synthesis 2111:Lineweaver–Burk plot 1922:Homocitrate synthase 1809:Peptidyl transferase 413:ATP citrate synthase 35:ATP citrate synthase 2528:Enoyl CoA isomerase 2482:Enoyl-CoA hydratase 2346:Enoyl ACP reductase 2323:Fatty acid synthase 1654:N-acetyltransferase 1497:10.1021/ja01115a547 1179:2019Natur.568..566W 822:2019Natur.568..571V 738:Chlorobium limicola 435:, the enzyme links 2070:Enzyme superfamily 2003:Enzyme promiscuity 1614:acetyltransferases 1526:, which is in the 1428:10.1002/prot.10286 2643:Citric acid cycle 2620: 2619: 2616: 2615: 2575: 2574: 2394: 2393: 2303:ATP citrate lyase 2226: 2225: 1935: 1934: 1885:ATP citrate lyase 1511:ATP Citrate Lyase 1371:(11): 1022–1032. 1173:(7753): 566–570. 1095:(15): 3709–3714. 1067:ATP+Citrate+Lyase 981:10.1104/pp.008110 816:(7753): 571–575. 726:X-ray diffraction 492:cholesterogenesis 410: 409: 406: 405: 229: 228: 225: 224: 128:metabolic pathway 18:ATP citrate lyase 16:(Redirected from 2650: 2442: 2405: 2374:Triacyl glycerol 2290: 2264:lipid metabolism 2253: 2246: 2239: 2230: 2106:Hanes–Woolf plot 2049:Enzyme activator 2044:Enzyme inhibitor 2018:Enzyme catalysis 1962: 1955: 1948: 1939: 1895:HMG-CoA synthase 1850:Citrate synthase 1814:Transglutaminase 1591:acyltransferases 1580: 1573: 1566: 1557: 1548: 1547: 1539: 1500: 1479: 1447: 1401: 1400: 1390: 1380: 1356: 1350: 1349: 1339: 1329: 1305: 1299: 1298: 1288: 1256: 1250: 1249: 1213: 1207: 1206: 1162: 1156: 1155: 1145: 1121: 1115: 1114: 1104: 1080: 1074: 1064: 1058: 1057: 1047: 1038:(49): 35657–65. 1023: 1017: 1016: 1009: 1003: 1002: 992: 969:Plant Physiology 960: 947: 946: 936: 926: 917:(35): 27418–28. 902: 891: 890: 880: 856: 850: 849: 807: 798: 756:citryl-CoA lyase 560:brassinosteroids 427:. By converting 379: 243: 231: 182: 32: 27:Class of enzymes 21: 2658: 2657: 2653: 2652: 2651: 2649: 2648: 2647: 2623: 2622: 2621: 2612: 2594: 2571: 2555: 2537: 2514: 2431: 2390: 2369: 2350: 2321: 2312: 2281: 2257: 2227: 2222: 2134:Oxidoreductases 2120: 2096:Enzyme kinetics 2084: 2080:List of enzymes 2053: 2022: 1993:Catalytic triad 1971: 1966: 1936: 1931: 1890:Malate synthase 1835: 1786: 1598: 1584: 1554: 1542: 1534: 1507: 1482: 1453: 1450: 1413: 1409: 1407:Further reading 1404: 1358: 1357: 1353: 1307: 1306: 1302: 1258: 1257: 1253: 1215: 1214: 1210: 1164: 1163: 1159: 1130:Cell Metabolism 1123: 1122: 1118: 1089:Cancer Research 1082: 1081: 1077: 1065: 1061: 1025: 1024: 1020: 1011: 1010: 1006: 962: 961: 950: 904: 903: 894: 858: 857: 853: 805: 800: 799: 788: 784: 772:LDL cholesterol 764: 651:Marchantimorpha 639: 627: 613: 605: 572: 473: 246: 28: 23: 22: 15: 12: 11: 5: 2656: 2654: 2646: 2645: 2640: 2635: 2625: 2624: 2618: 2617: 2614: 2613: 2611: 2610: 2604: 2602: 2596: 2595: 2593: 2592: 2586: 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2337: 2334: 2332: 2329: 2328: 2326: 2324: 2319: 2315: 2309: 2306: 2304: 2301: 2300: 2298: 2295: 2291: 2288: 2284: 2280: 2277: 2273: 2269: 2265: 2261: 2254: 2249: 2247: 2242: 2240: 2235: 2234: 2231: 2218: 2214: 2213: 2208: 2205: 2201: 2200: 2195: 2192: 2188: 2187: 2182: 2179: 2175: 2174: 2169: 2166: 2162: 2161: 2156: 2153: 2149: 2148: 2143: 2140: 2136: 2135: 2130: 2129: 2127: 2123: 2117: 2114: 2112: 2109: 2107: 2104: 2102: 2099: 2097: 2094: 2093: 2091: 2087: 2081: 2078: 2076: 2075:Enzyme family 2073: 2071: 2068: 2066: 2063: 2062: 2060: 2056: 2050: 2047: 2045: 2042: 2040: 2039:Cooperativity 2037: 2035: 2032: 2031: 2029: 2025: 2019: 2016: 2014: 2011: 2009: 2006: 2004: 2001: 1999: 1998:Oxyanion hole 1996: 1994: 1991: 1989: 1986: 1984: 1981: 1980: 1978: 1974: 1970: 1963: 1958: 1956: 1951: 1949: 1944: 1943: 1940: 1928: 1925: 1923: 1920: 1918: 1915: 1913: 1910: 1908: 1905: 1901: 1898: 1897: 1896: 1893: 1891: 1888: 1886: 1883: 1881: 1878: 1876: 1873: 1871: 1868: 1866: 1863: 1861: 1858: 1856: 1853: 1851: 1848: 1847: 1845: 1842: 1838: 1830: 1827: 1825: 1822: 1820: 1817: 1816: 1815: 1812: 1810: 1807: 1805: 1802: 1801: 1799: 1797: 1793: 1789: 1783: 1780: 1778: 1775: 1773: 1770: 1768: 1765: 1764: 1761: 1758: 1756: 1753: 1751: 1748: 1746: 1743: 1741: 1738: 1735: 1734: 1729: 1726: 1724: 1721: 1720: 1719: 1716: 1712: 1709: 1707: 1704: 1703: 1702: 1699: 1697: 1693: 1692: 1687: 1684: 1682: 1679: 1678: 1677: 1674: 1670: 1667: 1665: 1662: 1660: 1657: 1656: 1655: 1652: 1650: 1647: 1645: 1642: 1640: 1637: 1635: 1632: 1630: 1627: 1625: 1622: 1620: 1617: 1615: 1611: 1610: 1608: 1605: 1601: 1596: 1592: 1588: 1581: 1576: 1574: 1569: 1567: 1562: 1561: 1558: 1551: 1546: 1541: 1537: 1532: 1531: 1529: 1528:public domain 1525: 1516: 1512: 1509: 1508: 1504: 1498: 1494: 1490: 1486: 1481: 1477: 1473: 1469: 1465: 1462:(3): 645–50. 1461: 1457: 1452: 1451: 1445: 1441: 1437: 1433: 1429: 1425: 1422:(3): 437–50. 1421: 1417: 1412: 1411: 1406: 1398: 1394: 1389: 1388:10044/1/68213 1384: 1379: 1374: 1370: 1366: 1362: 1355: 1352: 1347: 1343: 1338: 1333: 1328: 1323: 1319: 1315: 1311: 1304: 1301: 1296: 1292: 1287: 1282: 1278: 1274: 1270: 1266: 1262: 1255: 1252: 1247: 1243: 1239: 1235: 1231: 1227: 1224:(3): 763–70. 1223: 1219: 1212: 1209: 1204: 1200: 1196: 1192: 1188: 1184: 1180: 1176: 1172: 1168: 1161: 1158: 1153: 1149: 1144: 1139: 1135: 1131: 1127: 1120: 1117: 1112: 1108: 1103: 1098: 1094: 1090: 1086: 1079: 1076: 1072: 1068: 1063: 1060: 1055: 1051: 1046: 1041: 1037: 1033: 1029: 1022: 1019: 1014: 1008: 1005: 1000: 996: 991: 986: 982: 978: 975:(2): 740–56. 974: 970: 966: 959: 957: 955: 953: 949: 944: 940: 935: 930: 925: 920: 916: 912: 908: 901: 899: 897: 893: 888: 884: 879: 874: 870: 866: 862: 855: 852: 847: 843: 839: 835: 831: 827: 823: 819: 815: 811: 804: 797: 795: 793: 791: 787: 781: 779: 777: 773: 769: 761: 759: 757: 753: 749: 748: 744: 740: 739: 735: 731: 727: 722: 720: 716: 712: 711:Rossmann fold 708: 703: 701: 697: 693: 688: 686: 682: 681: 680:Chlamydomonas 676: 672: 668: 664: 660: 656: 652: 648: 647:Chlorophyceae 644: 636: 634: 632: 624: 622: 620: 609: 608: 607: 601: 597: 593: 589: 585: 581: 577: 569: 567: 565: 561: 557: 553: 549: 545: 541: 537: 533: 530:; acetylated 529: 525: 521: 517: 513: 509: 508:sphingolipids 505: 501: 500:phospholipids 495: 493: 489: 485: 481: 478: 470: 468: 466: 462: 458: 454: 450: 446: 442: 438: 434: 430: 426: 422: 418: 414: 402: 399: 395: 392: 389: 385: 380: 376: 373: 372: 368: 365: 363: 359: 356: 353: 351: 347: 342: 339: 336: 334: 330: 327: 324: 322: 318: 315: 312: 310: 306: 303: 300: 298: 294: 291: 288: 286: 282: 279: 276: 274: 270: 266: 262: 258: 254: 249: 242: 237: 232: 221: 218: 216: 212: 209: 206: 204: 200: 197: 194: 192: 188: 183: 179: 176: 172: 169: 167: 166:Gene Ontology 163: 160: 157: 154: 151: 148: 144: 141: 138: 136: 132: 129: 126: 124: 120: 117: 114: 112: 108: 105: 104:NiceZyme view 102: 100: 96: 93: 90: 88: 84: 81: 78: 76: 72: 67: 64: 61: 59: 55: 52: 49: 47: 43: 38: 33: 30: 19: 2272:triglyceride 2212:Translocases 2209: 2196: 2183: 2170: 2157: 2147:Transferases 2144: 2131: 1988:Binding site 1736: 1694: 1612: 1587:Transferases 1521: 1520: 1491:(19): 4874. 1488: 1484: 1459: 1455: 1419: 1415: 1368: 1364: 1354: 1317: 1313: 1303: 1271:(1): 33–41. 1268: 1264: 1254: 1221: 1217: 1211: 1170: 1166: 1160: 1133: 1129: 1119: 1092: 1088: 1078: 1062: 1035: 1031: 1021: 1007: 972: 968: 914: 910: 871:(2): 491–9. 868: 864: 854: 813: 809: 765: 762:Pharmacology 745: 736: 723: 704: 699: 695: 689: 678: 675:glaucophytes 643:green plants 640: 628: 616: 592:oxaloacetate 580:oxaloacetate 573: 544:anthocyanins 528:malonic acid 506:moieties of 496: 474: 455:, including 441:intermediate 416: 412: 411: 369: 264:Alt. symbols 92:BRENDA entry 29: 2520:Unsaturated 2400:Degradation 2357:desaturases 2355:Fatty acid 2294:Malonyl-CoA 1983:Active site 1829:Factor XIII 719:active site 685:prokaryotes 645:(including 598:(ADP), and 558:, sterols, 552:isoprenoids 540:isoprenoids 488:lipogenesis 465:polyketides 453:metabolites 391:Swiss-model 251:Identifiers 80:IntEnz view 40:Identifiers 2627:Categories 2582:acetyl-CoA 2386:Thiokinase 2276:fatty acid 2260:Metabolism 2186:Isomerases 2160:Hydrolases 2027:Regulation 782:References 715:C-terminal 707:N-terminal 576:Coenzyme A 524:flavonoids 480:acetyl-CoA 433:acetyl-CoA 387:Structures 382:Search for 344:Other data 149:structures 116:KEGG entry 63:9027-95-6 2600:Aldehydes 2543:Odd chain 2296:synthesis 2286:Synthesis 2065:EC number 655:Bryopsida 637:Structure 631:cytosolic 621:4.1.3.8. 619:EC number 536:alkaloids 532:phenolics 477:cytosolic 449:cytosolic 350:EC number 326:NM_001096 273:NCBI gene 69:Databases 2638:EC 2.3.3 2089:Kinetics 2013:Cofactor 1976:Activity 1681:P300/CBP 1436:12557186 1416:Proteins 1397:30865796 1346:32242119 1295:31873304 1246:32105039 1238:15101982 1203:93000843 1195:30944472 1152:26039447 1111:22787121 1054:17928289 999:12376641 943:20558738 846:92999924 838:30944476 743:archaeon 741:and the 667:eudicots 659:Pinaceae 625:Location 570:Reaction 564:plastids 504:ceramide 484:tetramer 471:Function 419:) is an 401:InterPro 220:proteins 208:articles 196:articles 153:RCSB PDB 2445:General 2279:enzymes 2199:Ligases 1969:Enzymes 1550:Biology 1476:6749502 1444:8358424 1337:8439269 1286:8436250 1175:Bibcode 934:2930740 887:1371749 818:Bibcode 694:of the 588:citrate 554:(e.g., 520:suberin 512:cuticle 461:sterols 443:, with 429:citrate 397:Domains 367:Chr. 17 355:2.3.3.8 333:UniProt 175:QuickGO 140:profile 123:MetaCyc 58:CAS no. 51:2.3.3.8 2476:ACADSB 2471:ACADVL 2173:Lyases 1900:HMGCS2 1737:other: 1728:SPTLC2 1723:SPTLC1 1664:HGSNAT 1536:Portal 1517:(MeSH) 1474:  1442:  1434:  1395:  1344:  1334:  1293:  1283:  1244:  1236:  1201:  1193:  1167:Nature 1150:  1109:  1073:(MeSH) 1052:  997:  990:166603 987:  941:  931:  885:  844:  836:  810:Nature 692:fusion 683:, and 665:, and 548:sugars 546:, and 518:, and 502:, the 463:, and 421:enzyme 415:(also 338:P53396 321:RefSeq 302:108728 256:Symbol 203:PubMed 185:Search 171:AmiGO 159:PDBsum 99:ExPASy 87:BRENDA 75:IntEnz 46:EC no. 2560:Other 2503:HADHB 2498:HADHA 2466:ACADS 2461:ACADM 2456:ACADL 2125:Types 1841:2.3.3 1792:2.3.2 1782:ABHD5 1669:ARD1A 1604:2.3.1 1440:S2CID 1242:S2CID 1199:S2CID 842:S2CID 806:(PDF) 671:fungi 516:cutin 457:waxes 371:q21.2 362:Locus 135:PRIAM 2493:HADH 2274:and 2217:list 2210:EC7 2204:list 2197:EC6 2191:list 2184:EC5 2178:list 2171:EC4 2165:list 2158:EC3 2152:list 2145:EC2 2139:list 2132:EC1 1711:CPT2 1706:CPT1 1686:NAT2 1597:2.3) 1472:PMID 1432:PMID 1393:PMID 1342:PMID 1291:PMID 1234:PMID 1191:PMID 1148:PMID 1107:PMID 1050:PMID 995:PMID 939:PMID 883:PMID 834:PMID 700:ACLB 698:and 696:ACLA 490:and 297:OMIM 285:HGNC 259:ACLY 215:NCBI 156:PDBe 111:KEGG 2580:To 2489:MTP 1493:doi 1464:doi 1460:125 1424:doi 1383:hdl 1373:doi 1369:380 1332:PMC 1322:doi 1281:PMC 1273:doi 1226:doi 1183:doi 1171:568 1138:doi 1097:doi 1040:doi 1036:282 985:PMC 977:doi 973:130 929:PMC 919:doi 915:285 873:doi 869:204 826:doi 814:568 606:): 584:ATP 522:); 431:to 309:PDB 290:115 267:ACL 191:PMC 147:PDB 2629:: 2491:: 2270:, 2266:/ 2262:: 1794:: 1595:EC 1589:: 1489:75 1487:. 1470:. 1458:. 1438:. 1430:. 1420:50 1418:. 1391:. 1381:. 1367:. 1363:. 1340:. 1330:. 1318:27 1316:. 1312:. 1289:. 1279:. 1269:27 1267:. 1263:. 1240:. 1232:. 1222:52 1220:. 1197:. 1189:. 1181:. 1169:. 1146:. 1134:21 1132:. 1128:. 1105:. 1093:72 1091:. 1087:. 1048:. 1034:. 1030:. 993:. 983:. 971:. 967:. 951:^ 937:. 927:. 913:. 909:. 895:^ 881:. 867:. 863:. 840:. 832:. 824:. 812:. 808:. 789:^ 687:. 677:, 673:, 661:, 657:, 653:, 649:, 602:(P 594:, 542:, 538:, 534:, 526:; 514:, 510:, 467:. 459:, 278:47 173:/ 2478:) 2454:( 2320:/ 2252:e 2245:t 2238:v 2219:) 2215:( 2206:) 2202:( 2193:) 2189:( 2180:) 2176:( 2167:) 2163:( 2154:) 2150:( 2141:) 2137:( 1961:e 1954:t 1947:v 1698:: 1616:: 1593:( 1579:e 1572:t 1565:v 1538:: 1530:. 1499:. 1495:: 1478:. 1466:: 1446:. 1426:: 1399:. 1385:: 1375:: 1348:. 1324:: 1297:. 1275:: 1248:. 1228:: 1205:. 1185:: 1177:: 1154:. 1140:: 1113:. 1099:: 1056:. 1042:: 1015:. 1001:. 979:: 945:. 921:: 889:. 875:: 848:. 828:: 820:: 730:Ă… 612:i 604:i 20:)

Index

ATP citrate lyase
EC no.
2.3.3.8
CAS no.
9027-95-6
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB
RCSB PDB
PDBe
PDBsum
Gene Ontology
AmiGO
QuickGO
PMC
articles
PubMed
articles
NCBI
proteins

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