569:
622:
941:
245:
29:
773:
Mostly consuming tissues such as heart and brain have more ATP-specific succinyl-CoA synthetase (ATPSCS), while synthetic tissues such as kidney and liver have the more GTP-specific form (GTPSCS). Kinetics analysis of ATPSCS from the breast muscle of pigeons and GTPSCS from pigeon liver showed that
808:
cells showed that GTP specific SCSs were located in pigeon liver cells, and ATP specific SCSs were located in the pigeon breast muscle cells. Further research revealed a similar phenomenon of GTP and ATP specific SCSs in rat, mouse, and human tissue. It appears that tissue typically involved in
617:
and characterized in great detail. As can be seen in Image 2, the two α subunits (pink and green) reside on opposite sides of the structure and the two β subunits (yellow and blue) interact in the middle region of the protein. The two α subunits only interact with a single β unit, whereas the β
542:
where Pi denotes inorganic phosphate, NDP denotes nucleotide diphosphate (either GDP or ADP), and NTP denotes nucleotide triphosphate (either GTP or ATP). As mentioned, the enzyme facilitates coupling of the conversion of succinyl CoA to succinate with the formation of NTP from NDP and Pi. The
683:) in close proximity to a histidine residue (His246α). This histidine residue becomes phosphorylated during the succinate forming step in the reaction mechanism. The exact binding location of succinate is not well-defined. The formation of the nucleotide triphosphate occurs in an
910:, which is a disease in infants that is characterized by the build-up of toxic levels of lactic acid. The condition (when it is most severe) results in death usually within 2–4 days after birth. It has been determined that patients with the condition display a two
704:
residues (one near the catalytic histidine, Glu208α and one near the ATP grasp domain, Glu197β) play a role in the phosphorylation and dephosphorylation of the histidine, but the exact mechanism by which the enzyme changes conformation is not fully understood.
563:
residue to remove the phosphate group from succinyl phosphate and generate succinate. Finally, the phosphorylated histidine transfers the phosphate group to a nucleoside diphosphate, which generates the high-energy carrying nucleoside triphosphate.
803:
SCSs can catalyze either GTP or ATP formation. However, mammals possess different types of SCSs that are specific for either GTP (G-SCS) or ATP (A-SCS) and are native to different types of tissue within the organism. An interesting study using
1300:
Fraser ME, Joyce MA, Ryan DG, Wolodko WT (Jan 2002). "Two glutamate residues, Glu 208 alpha and Glu 197 beta, are crucial for phosphorylation and dephosphorylation of the active-site histidine residue in succinyl-CoA synthetase".
1177:
Wolodko WT, Kay CM, Bridger WA (Sep 1986). "Active enzyme sedimentation, sedimentation velocity, and sedimentation equilibrium studies of succinyl-CoA synthetases of porcine heart and
Escherichia coli".
691:
of the each β subunit. However, this grasp domain is located about 35 Å away from the phosphorylated histidine residue. This leads researchers to believe that the enzyme must undergo a major change in
1615:
Hunger-Glaser I, Brun R, Linder M, Seebeck T (May 1999). "Inhibition of succinyl CoA synthetase histidine-phosphorylation in
Trypanosoma brucei by an inhibitor of bacterial two-component systems".
618:
units interact with a single α unit (to form the αβ dimer) and the β subunit of the other αβ dimer. A short amino acid chain links the two β subunits which gives rise to the tetrameric structure.
1772:
568:
1650:
Wider de Xifra E, del C Batlle AM (Mar 1978). "Porphyrin biosynthesis: immobilized enzymes and ligands. VI. Studies on succinyl CoA synthetase from cultured soya bean cells".
2148:
2111:
419:
199:
1765:
1262:
Joyce MA, Fraser ME, James MN, Bridger WA, Wolodko WT (Jan 2000). "ADP-binding site of
Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography".
2953:
2045:
438:
218:
1541:"Distinct physiological roles of animal succinate thiokinases. Association of guanine nucleotide-linked succinate thiokinase with ketone body utilization"
2629:
1758:
3018:
3210:
2624:
2715:
2297:
2016:
3158:
969:
964:
833:
by controlling the interconversion between succinyl CoA and succinate. This is important because succinyl CoA is an intermediate necessary for
2383:
1077:
3124:
2192:
925:
and the citric acid cycle. Since the cells do not have a functional citric acid cycle, acidosis results because cells are forced to choose
2141:
1030:
Fraser ME, James MN, Bridger WA, Wolodko WT (Jan 1999). "A detailed structural description of
Escherichia coli succinyl-CoA synthetase".
1690:"Deficiency of the alpha subunit of succinate-coenzyme A ligase causes fatal infantile lactic acidosis with mitochondrial DNA depletion"
795:
SCS is the only enzyme in the citric acid cycle that catalyzes a reaction in which a nucleotide triphosphate (GTP or ATP) is formed by
656:
of
Succinyl-CoA synthetase alpha subunit (succinyl-CoA-binding isoform) was determined by Joyce et al. to a resolution of 2.10 A, with
2946:
2483:
2418:
1898:
1817:
3270:
2428:
2253:
1148:
1115:
865:
1430:"Characterization of the ATP- and GTP-specific succinyl-CoA synthetases in pigeon. The enzymes incorporate the same alpha-subunit"
921:
that encodes the α subunit of SCS. As a result, functional SCS is absent in metabolism causing a major imbalance in flux between
3225:
2754:
2552:
2187:
431:
211:
3230:
2921:
2749:
2413:
2134:
796:
778:
were similar for CoA, but different for the nucleotides, phosphate, and succinate. The largest difference was for succinate: K
758:
phosphates is defined by the β-subunit, which is encoded by 2 genes. SUCLG2 is GTP-specific and SUCLA2 is ATP-specific, while
3220:
2744:
2530:
2055:
1885:
1873:
358:
138:
3426:
3237:
3063:
382:
162:
2939:
1894:
895:
Measurements (performed using a soy bean SCS) indicate an optimal temperature of 37 °C and an optimal pH of 7.0-8.0.
2334:
2276:
2166:
1881:
1469:
Labbe RF, Kurumada T, Onisawa J (Dec 1965). "The role of succinyl-CoA synthetase in the control of heme biosynthesis".
2388:
3083:
3058:
3043:
3003:
3205:
3200:
3173:
2562:
2557:
2361:
2227:
1345:"Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes"
857:
3411:
3119:
3078:
3038:
3028:
3023:
3008:
609:
structure. However, mammalian mitochondrial SCSs are active as αβ dimers and do not form a heterotetramer. The
3527:
3514:
3501:
3488:
3475:
3462:
3449:
3195:
3134:
3105:
2988:
2979:
2287:
1982:
3421:
3088:
3013:
2998:
3375:
3318:
2970:
2478:
2356:
1977:
1937:
1812:
1744:
926:
861:
733:
721:
376:
269:
156:
49:
3068:
3048:
3033:
2993:
3323:
2525:
2312:
2002:
1918:
1829:
959:
873:
653:
614:
487:
363:
143:
3093:
3073:
3053:
1740:
3185:
2520:
2177:
1961:
1910:
1877:
1131:
Nishimura JS (1986). "Succinyl-CoA synthetase structure-function relationships and other considerations".
767:
763:
495:
491:
1389:"Expression of two succinyl-CoA synthetases with different nucleotide specificities in mammalian tissues"
762:
encodes the common α-subunit. β variants are produced at different amounts in different tissues, causing
696:
to bring the histidine to the grasp domain and facilitate the formation of the nucleoside triphosphate.
3344:
3263:
3215:
2894:
2634:
2510:
2346:
2324:
1855:
621:
507:
503:
443:
223:
3416:
1098:
Berg, Jeremy M. (Jeremy M.); Tymoczko, John L.; Stryer, Lubert.; Stryer, Lubert. Biochemistry. (2002).
351:
131:
879:. This operon is up-regulated by the presence of oxygen and responds to a variety of carbon sources.
3143:
2735:
2641:
2498:
2447:
2393:
2026:
1956:
1844:
693:
519:
286:
66:
1688:
Ostergaard E, Christensen E, Kristensen E, Mogensen B, Duno M, Shoubridge EA, Wibrand F (Aug 2007).
3549:
3380:
2106:
531:
499:
281:
61:
379:
159:
3313:
2665:
2433:
2307:
1997:
1570:
830:
775:
548:
303:
83:
1135:. Advances in Enzymology and Related Areas of Molecular Biology. Vol. 58. pp. 141–72.
3554:
2655:
2458:
2239:
1785:
1719:
1667:
1632:
1597:
1562:
1521:
1486:
1451:
1410:
1366:
1318:
1279:
1241:
1195:
1154:
1144:
1111:
1107:
1073:
1047:
1012:
954:
914:
884:
676:
657:
544:
511:
370:
150:
2931:
1504:
Ottaway JH, McClellan JA, Saunderson CL (1981). "Succinic thiokinase and metabolic control".
1344:
3359:
3354:
3328:
3256:
3148:
2468:
2261:
2080:
2075:
1948:
1802:
1709:
1701:
1659:
1624:
1552:
1513:
1478:
1441:
1400:
1356:
1310:
1271:
1231:
1187:
1136:
1039:
1002:
590:
3406:
3390:
3303:
2373:
2266:
907:
648:. Pink and yellow form the one dimer and green and blue form the other dimer. PDB ID: 1CQG
585:
339:
119:
860:
at the transcriptional level. It has been demonstrated that the gene for SCS (sucCD) is
1750:
315:
95:
3444:
3385:
3190:
1714:
1689:
991:"Interactions of GTP with the ATP-grasp domain of GTP-specific succinyl-CoA synthetase"
946:
826:
606:
414:
274:
194:
54:
1628:
661:
394:
174:
3543:
3349:
3308:
2157:
1663:
1557:
1540:
1517:
1482:
1100:
880:
869:
680:
595:
559:
inorganic phosphate molecule to form succinyl phosphate. The enzyme then utilizes a
389:
169:
1574:
3298:
2790:
2765:
2423:
2302:
2215:
2021:
2007:
1929:
845:
479:
883:
that prevent phosphorylation of histidine, like the molecule LY26650, are potent
3522:
3457:
3293:
842:
747:
697:
556:
398:
178:
1220:"A detailed structural description of escherichia coli succinly-CoA synthetase"
940:
551:
which is depicted in the image below. The first step involves displacement of
2542:
2204:
1865:
1781:
1140:
936:
922:
814:
688:
552:
515:
486:. The enzyme facilitates the coupling of this reaction to the formation of a
1446:
1429:
1361:
3496:
3470:
2473:
1807:
911:
834:
810:
755:
751:
701:
684:
560:
483:
475:
255:
35:
1723:
1636:
1414:
1405:
1388:
1322:
1283:
1245:
1236:
1219:
1043:
1016:
1007:
990:
1566:
1525:
1490:
1455:
1370:
1199:
1158:
1051:
2619:
2493:
2126:
1839:
1671:
1601:
1191:
2779:
2774:
2694:
813:(like the liver and kidneys) express G-SCS, whereas tissue involved in
736:
724:
714:
346:
327:
126:
107:
1314:
1275:
3509:
3279:
3153:
2966:
2962:
2884:
2879:
2849:
2844:
2724:
2704:
2699:
2689:
2684:
2679:
2674:
1788:
918:
876:
805:
759:
740:
728:
717:, one that specifies synthesis of ATP, and one that synthesises GTP.
426:
322:
310:
298:
206:
102:
90:
78:
1705:
1387:
Lambeth DO, Tews KN, Adkins S, Frohlich D, Milavetz BI (Aug 2004).
713:
Johnson et al. describe two isoforms of succinyl-CoA synthetase in
3483:
3163:
2904:
2899:
2889:
2874:
2869:
2864:
2859:
2854:
2839:
2834:
2829:
2824:
2819:
2814:
2809:
2804:
2799:
2595:
2582:
2090:
2085:
1343:
Johnson JD, Mehus JG, Tews K, Milavetz BI, Lambeth DO (Oct 1998).
620:
547:
change of -3.4 kJ/mol. The reaction takes place by a three-step
3178:
3168:
2070:
2065:
2060:
2050:
2040:
1833:
989:
Fraser ME, Hayakawa K, Hume MS, Ryan DG, Brownie ER (Apr 2006).
838:
817:(like the brain, the heart, and muscular tissue) express A-SCS.
510:). It plays a key role as one of the catalysts involved in the
334:
114:
3252:
2935:
2130:
1754:
244:
28:
1133:
Advances in
Enzymology and Related Areas of Molecular Biology
3248:
1218:
Fraser ME, James MN, Bridger WA, Wolodko J (May 1999).
502:
molecule and a nucleoside diphosphate molecule (either
33:
Pig GTP-specific succinyl-CoA synthetase with GTP. PDB
1471:
Biochimica et
Biophysica Acta (BBA) - General Subjects
750:
of an α- and a β-subunit. The specificity for either
632:
584:
Bacterial and mammalian SCSs are made up of α and β
3435:
3399:
3368:
3337:
3286:
3133:
3104:
2978:
2788:
2763:
2733:
2713:
2663:
2654:
2608:
2571:
2539:
2507:
2455:
2446:
2402:
2370:
2343:
2321:
2284:
2275:
2252:
2224:
2201:
2174:
2165:
2099:
1990:
1974:
1946:
1927:
1908:
1863:
1854:
1795:
1070:
Biochemistry / Donald J. Voet ; Judith G. Voet
782:app of ATPSCS = 5mM versus that of GTPSCS = 0.5mM.
437:
425:
413:
408:
388:
369:
357:
345:
333:
321:
309:
297:
292:
280:
268:
263:
237:
217:
205:
193:
188:
168:
149:
137:
125:
113:
101:
89:
77:
72:
60:
48:
43:
21:
1683:
1681:
1099:
538:Succinyl CoA + Pi + NDP ↔ Succinate + CoA + NTP
2112:Electron-transferring-flavoprotein dehydrogenase
906:Defective SCS has been implicated as a cause of
530:Succinyl CoA synthetase catalyzes the following
2017:Complex III/Coenzyme Q - cytochrome c reductase
1428:Johnson JD, Muhonen WW, Lambeth DO (Oct 1998).
1382:
1380:
1338:
1336:
1334:
1332:
1172:
1170:
1168:
3264:
2947:
2142:
1766:
1295:
1293:
1213:
1211:
1209:
8:
1257:
1255:
3271:
3257:
3249:
2954:
2940:
2932:
2660:
2630:Mitochondrial permeability transition pore
2612:
2452:
2281:
2171:
2149:
2135:
2127:
1987:
1860:
1773:
1759:
1751:
543:reaction has a biochemical standard state
405:
243:
185:
27:
1743:at the U.S. National Library of Medicine
1713:
1556:
1506:The International Journal of Biochemistry
1445:
1404:
1360:
1235:
1006:
675:SCS provide evidence that the coenzyme A
2625:Mitochondrial membrane transport protein
1588:Kruspl W, Streitmann B (Feb 1975). "".
981:
929:as the primary means of producing ATP.
2384:Cholesterol side-chain cleavage enzyme
1617:Molecular and Biochemical Parasitology
1093:
1091:
1089:
1063:
1061:
791:Generation of nucleotide triphosphates
526:Chemical reaction and enzyme mechanism
234:
18:
3019:D-alanine—poly(phosphoribitol) ligase
700:experiments have determined that two
7:
1539:Jenkins TM, Weitzman PD (Sep 1986).
821:Formation of metabolic intermediates
799:. Research studies have shown that
2298:Coenzyme Q – cytochrome c reductase
1434:The Journal of Biological Chemistry
1393:The Journal of Biological Chemistry
1349:The Journal of Biological Chemistry
1106:. New York: W.H. Freeman. pp.
995:The Journal of Biological Chemistry
3159:Von Hippel–Lindau tumor suppressor
2484:Oxoglutarate dehydrogenase complex
2419:Glycerol-3-phosphate dehydrogenase
2003:Complex II/Succinate dehydrogenase
1899:Pyruvate dehydrogenase phosphatase
1694:American Journal of Human Genetics
970:Succinate—CoA ligase (GDP-forming)
965:Succinate—CoA ligase (ADP-forming)
872:called sdhC, which is part of the
687:domain, which is located near the
238:Succinate—CoA ligase (ADP-forming)
22:Succinate—CoA ligase (GDP-forming)
14:
2429:Carnitine palmitoyltransferase II
3125:Long-chain-fatty-acid—CoA ligase
2553:Carbamoyl phosphate synthetase I
2193:Long-chain-fatty-acid—CoA ligase
2188:Carnitine palmitoyltransferase I
939:
904:Fatal infantile lactic acidosis:
856:In some bacteria, the enzyme is
679:within each α-subunit (within a
567:
2414:Glutamate aspartate transporter
2027:Complex IV/Cytochrome c oxidase
1741:Succinyl+Coenzyme+A+Synthetases
1590:Zeitschrift fĂĽr Hautkrankheiten
908:fatal infantile lactic acidosis
868:(sucAB) under the control of a
797:substrate-level phosphorylation
518:, and it is located within the
3221:Carbamoyl phosphate synthetase
3115:Succinyl coenzyme A synthetase
2531:Pyruvate dehydrogenase complex
2489:Succinyl coenzyme A synthetase
1874:Pyruvate dehydrogenase complex
456:Succinyl coenzyme A synthetase
1:
1895:Pyruvate dehydrogenase kinase
1652:Biochimica et Biophysica Acta
1629:10.1016/s0166-6851(99)00032-8
866:α-ketoglutarate dehydrogenase
746:In amniotes, the enzyme is a
249:Succinyl-COA synthetase from
2335:Dihydroorotate dehydrogenase
1998:Complex I/NADH dehydrogenase
1664:10.1016/0005-2744(78)90027-x
1558:10.1016/0014-5793(86)80900-0
1518:10.1016/0020-711x(81)90111-7
1483:10.1016/0304-4165(65)90050-4
1224:Journal of Molecular Biology
1032:Journal of Molecular Biology
613:SCS heterotetramer has been
2389:Steroid 11-beta-hydroxylase
671:Crystal structures for the
478:the reversible reaction of
3571:
3206:Holocarboxylase synthetase
3201:Argininosuccinate synthase
3174:Anaphase-promoting complex
2563:N-Acetylglutamate synthase
2558:Ornithine transcarbamylase
2362:Glycerol phosphate shuttle
2228:monoamine neurotransmitter
1818:Oxoglutarate dehydrogenase
1072:. New York, NY: Wiley, J.
598:link together to form an α
3427:Michaelis–Menten kinetics
3238:Glutamate–cysteine ligase
3196:Adenylosuccinate synthase
2989:Aminoacyl tRNA synthetase
2917:
2615:
2591:
2288:oxidative phosphorylation
1983:oxidative phosphorylation
1141:10.1002/9780470123041.ch4
917:within the gene known as
852:Regulation and inhibition
404:
242:
184:
26:
3319:Diffusion-limited enzyme
2479:Isocitrate dehydrogenase
2357:Malate-aspartate shuttle
1978:electron transport chain
1938:Methylmalonyl-CoA mutase
1813:Isocitrate dehydrogenase
1745:Medical Subject Headings
1447:10.1074/jbc.273.42.27573
1362:10.1074/jbc.273.42.27580
1068:Voet, Donald J. (2011).
864:along with the gene for
829:of molecules into other
770:substrate requirements.
2526:Glutamate dehydrogenase
2313:Succinate dehydrogenase
1919:Glutamate dehydrogenase
1830:Succinate dehydrogenase
1823:Succinyl CoA synthetase
960:Succinate dehydrogenase
874:succinate dehydrogenase
555:from succinyl CoA by a
514:, a central pathway in
488:nucleoside triphosphate
464:succinyl-CoA synthetase
3186:Glutathione synthetase
2922:mitochondrial diseases
2521:Aspartate transaminase
2178:fatty acid degradation
1962:Aspartate transaminase
1406:10.1074/jbc.M406884200
1237:10.1006/jmbi.1999.2773
1044:10.1006/jmbi.1998.2324
1008:10.1074/jbc.M511785200
927:lactic acid production
649:
3412:Eadie–Hofstee diagram
3345:Allosteric regulation
3216:Asparagine synthetase
3120:Acetyl—CoA synthetase
2635:Mitochondrial carrier
2511:anaplerotic reactions
2347:mitochondrial shuttle
2325:pyrimidine metabolism
624:
3422:Lineweaver–Burk plot
3144:Glutamine synthetase
2642:Translocator protein
2499:Malate dehydrogenase
2394:Aldosterone synthase
1957:Pyruvate carboxylase
1845:Malate dehydrogenase
825:SCS facilitates the
815:catabolic metabolism
520:mitochondrial matrix
474:) is an enzyme that
472:succinate-CoA ligase
468:succinate thiokinase
2254:Intermembrane space
2107:Alternative oxidase
1911:α-ketoglutaric acid
1192:10.1021/bi00367a012
887:of bacterial SCSs.
881:Antibacterial drugs
811:anabolic metabolism
776:Michaelis constants
532:reversible reaction
516:cellular metabolism
500:inorganic phosphate
3381:Enzyme superfamily
3314:Enzyme promiscuity
2609:Other/to be sorted
2574:alcohol metabolism
2434:Uncoupling protein
2308:NADH dehydrogenase
831:metabolic pathways
667:Catalytic residues
650:
3537:
3536:
3246:
3245:
3137:: Carbon-Nitrogen
2929:
2928:
2913:
2912:
2656:Mitochondrial DNA
2650:
2649:
2604:
2603:
2459:citric acid cycle
2442:
2441:
2248:
2247:
2240:Monoamine oxidase
2124:
2123:
2120:
2119:
1970:
1969:
1786:Citric acid cycle
1315:10.1021/bi011518y
1276:10.1021/bi991696f
1079:978-0-470-57095-1
955:Citric acid cycle
654:crystal structure
512:citric acid cycle
490:molecule (either
453:
452:
449:
448:
352:metabolic pathway
233:
232:
229:
228:
132:metabolic pathway
3562:
3417:Hanes–Woolf plot
3360:Enzyme activator
3355:Enzyme inhibitor
3329:Enzyme catalysis
3273:
3266:
3259:
3250:
3149:Ubiquitin ligase
2956:
2949:
2942:
2933:
2793:
2768:
2738:
2718:
2668:
2661:
2613:
2576:
2546:
2514:
2469:Citrate synthase
2462:
2453:
2407:
2377:
2350:
2328:
2291:
2282:
2262:Adenylate kinase
2233:
2209:
2181:
2172:
2151:
2144:
2137:
2128:
1988:
1949:oxaloacetic acid
1861:
1803:Citrate synthase
1775:
1768:
1761:
1752:
1728:
1727:
1717:
1685:
1676:
1675:
1647:
1641:
1640:
1612:
1606:
1605:
1585:
1579:
1578:
1560:
1536:
1530:
1529:
1501:
1495:
1494:
1466:
1460:
1459:
1449:
1425:
1419:
1418:
1408:
1384:
1375:
1374:
1364:
1340:
1327:
1326:
1297:
1288:
1287:
1259:
1250:
1249:
1239:
1215:
1204:
1203:
1174:
1163:
1162:
1128:
1122:
1121:
1105:
1095:
1084:
1083:
1065:
1056:
1055:
1027:
1021:
1020:
1010:
1001:(16): 11058–65.
986:
949:
944:
943:
891:Optimal activity
739:- GTP-forming -
727:- ATP-forming -
647:
643:
639:
635:
607:heterotetrameric
571:
462:, also known as
406:
258:
251:Escherichia coli
247:
235:
186:
38:
31:
19:
16:Class of enzymes
3570:
3569:
3565:
3564:
3563:
3561:
3560:
3559:
3540:
3539:
3538:
3533:
3445:Oxidoreductases
3431:
3407:Enzyme kinetics
3395:
3391:List of enzymes
3364:
3333:
3304:Catalytic triad
3282:
3277:
3247:
3242:
3129:
3108:: Carbon-Sulfur
3100:
2982:: Carbon-Oxygen
2974:
2965:: CO CS and CN
2960:
2930:
2925:
2909:
2789:
2784:
2764:
2759:
2734:
2729:
2714:
2709:
2664:
2646:
2600:
2587:
2572:
2567:
2540:
2535:
2508:
2503:
2456:
2438:
2403:
2398:
2374:steroidogenesis
2371:
2366:
2344:
2339:
2322:
2317:
2285:
2271:
2267:Creatine kinase
2244:
2230:
2225:
2220:
2202:
2197:
2175:
2161:
2155:
2125:
2116:
2095:
2037:
2011:
1981:
1976:
1966:
1942:
1923:
1904:
1850:
1791:
1779:
1737:
1732:
1731:
1687:
1686:
1679:
1649:
1648:
1644:
1614:
1613:
1609:
1587:
1586:
1582:
1538:
1537:
1533:
1503:
1502:
1498:
1468:
1467:
1463:
1440:(42): 27573–9.
1427:
1426:
1422:
1399:(35): 36621–4.
1386:
1385:
1378:
1355:(42): 27580–6.
1342:
1341:
1330:
1299:
1298:
1291:
1261:
1260:
1253:
1217:
1216:
1207:
1176:
1175:
1166:
1151:
1130:
1129:
1125:
1118:
1097:
1096:
1087:
1080:
1067:
1066:
1059:
1029:
1028:
1024:
988:
987:
983:
978:
945:
938:
935:
901:
899:Role in disease
893:
854:
823:
793:
788:
781:
774:their apparent
711:
669:
645:
641:
637:
633:
605:
601:
582:
577:
528:
259:
254:
39:
34:
17:
12:
11:
5:
3568:
3566:
3558:
3557:
3552:
3542:
3541:
3535:
3534:
3532:
3531:
3518:
3505:
3492:
3479:
3466:
3453:
3439:
3437:
3433:
3432:
3430:
3429:
3424:
3419:
3414:
3409:
3403:
3401:
3397:
3396:
3394:
3393:
3388:
3383:
3378:
3372:
3370:
3369:Classification
3366:
3365:
3363:
3362:
3357:
3352:
3347:
3341:
3339:
3335:
3334:
3332:
3331:
3326:
3321:
3316:
3311:
3306:
3301:
3296:
3290:
3288:
3284:
3283:
3278:
3276:
3275:
3268:
3261:
3253:
3244:
3243:
3241:
3240:
3235:
3234:
3233:
3228:
3218:
3213:
3208:
3203:
3198:
3193:
3191:CTP synthetase
3188:
3183:
3182:
3181:
3176:
3171:
3166:
3161:
3156:
3146:
3140:
3138:
3131:
3130:
3128:
3127:
3122:
3117:
3111:
3109:
3102:
3101:
3099:
3098:
3097:
3096:
3091:
3086:
3081:
3076:
3071:
3066:
3061:
3056:
3051:
3046:
3041:
3036:
3031:
3026:
3021:
3016:
3011:
3006:
3001:
2996:
2985:
2983:
2976:
2975:
2961:
2959:
2958:
2951:
2944:
2936:
2927:
2926:
2918:
2915:
2914:
2911:
2910:
2908:
2907:
2902:
2897:
2892:
2887:
2882:
2877:
2872:
2867:
2862:
2857:
2852:
2847:
2842:
2837:
2832:
2827:
2822:
2817:
2812:
2807:
2802:
2796:
2794:
2786:
2785:
2783:
2782:
2777:
2771:
2769:
2761:
2760:
2758:
2757:
2752:
2747:
2741:
2739:
2731:
2730:
2728:
2727:
2721:
2719:
2711:
2710:
2708:
2707:
2702:
2697:
2692:
2687:
2682:
2677:
2671:
2669:
2658:
2652:
2651:
2648:
2647:
2645:
2644:
2639:
2638:
2637:
2632:
2622:
2616:
2610:
2606:
2605:
2602:
2601:
2599:
2598:
2592:
2589:
2588:
2586:
2585:
2579:
2577:
2569:
2568:
2566:
2565:
2560:
2555:
2549:
2547:
2537:
2536:
2534:
2533:
2528:
2523:
2517:
2515:
2505:
2504:
2502:
2501:
2496:
2491:
2486:
2481:
2476:
2471:
2465:
2463:
2450:
2444:
2443:
2440:
2439:
2437:
2436:
2431:
2426:
2421:
2416:
2410:
2408:
2400:
2399:
2397:
2396:
2391:
2386:
2380:
2378:
2368:
2367:
2365:
2364:
2359:
2353:
2351:
2341:
2340:
2338:
2337:
2331:
2329:
2319:
2318:
2316:
2315:
2310:
2305:
2300:
2294:
2292:
2279:
2277:Inner membrane
2273:
2272:
2270:
2269:
2264:
2258:
2256:
2250:
2249:
2246:
2245:
2243:
2242:
2236:
2234:
2222:
2221:
2219:
2218:
2212:
2210:
2199:
2198:
2196:
2195:
2190:
2184:
2182:
2169:
2167:Outer membrane
2163:
2162:
2156:
2154:
2153:
2146:
2139:
2131:
2122:
2121:
2118:
2117:
2115:
2114:
2109:
2103:
2101:
2097:
2096:
2094:
2093:
2088:
2083:
2078:
2073:
2068:
2063:
2058:
2053:
2048:
2043:
2035:
2030:
2029:
2024:
2019:
2014:
2009:
2005:
2000:
1994:
1992:
1985:
1972:
1971:
1968:
1967:
1965:
1964:
1959:
1953:
1951:
1944:
1943:
1941:
1940:
1934:
1932:
1925:
1924:
1922:
1921:
1915:
1913:
1906:
1905:
1903:
1902:
1893:(regulated by
1890:
1889:
1870:
1868:
1858:
1852:
1851:
1849:
1848:
1842:
1837:
1826:
1825:
1820:
1815:
1810:
1805:
1799:
1797:
1793:
1792:
1780:
1778:
1777:
1770:
1763:
1755:
1749:
1748:
1736:
1735:External links
1733:
1730:
1729:
1706:10.1086/519222
1677:
1642:
1607:
1580:
1531:
1496:
1461:
1420:
1376:
1328:
1289:
1251:
1205:
1186:(19): 5420–5.
1164:
1149:
1123:
1116:
1085:
1078:
1057:
1038:(4): 1633–53.
1022:
980:
979:
977:
974:
973:
972:
967:
962:
957:
951:
950:
947:Biology portal
934:
931:
900:
897:
892:
889:
853:
850:
822:
819:
792:
789:
787:
784:
779:
744:
743:
731:
710:
707:
668:
665:
640:, β subunits:
603:
599:
581:
578:
576:
573:
540:
539:
527:
524:
451:
450:
447:
446:
441:
435:
434:
429:
423:
422:
417:
411:
410:
402:
401:
392:
386:
385:
374:
367:
366:
361:
355:
354:
349:
343:
342:
337:
331:
330:
325:
319:
318:
313:
307:
306:
301:
295:
294:
290:
289:
284:
278:
277:
272:
266:
265:
261:
260:
248:
240:
239:
231:
230:
227:
226:
221:
215:
214:
209:
203:
202:
197:
191:
190:
182:
181:
172:
166:
165:
154:
147:
146:
141:
135:
134:
129:
123:
122:
117:
111:
110:
105:
99:
98:
93:
87:
86:
81:
75:
74:
70:
69:
64:
58:
57:
52:
46:
45:
41:
40:
32:
24:
23:
15:
13:
10:
9:
6:
4:
3:
2:
3567:
3556:
3553:
3551:
3548:
3547:
3545:
3529:
3525:
3524:
3519:
3516:
3512:
3511:
3506:
3503:
3499:
3498:
3493:
3490:
3486:
3485:
3480:
3477:
3473:
3472:
3467:
3464:
3460:
3459:
3454:
3451:
3447:
3446:
3441:
3440:
3438:
3434:
3428:
3425:
3423:
3420:
3418:
3415:
3413:
3410:
3408:
3405:
3404:
3402:
3398:
3392:
3389:
3387:
3386:Enzyme family
3384:
3382:
3379:
3377:
3374:
3373:
3371:
3367:
3361:
3358:
3356:
3353:
3351:
3350:Cooperativity
3348:
3346:
3343:
3342:
3340:
3336:
3330:
3327:
3325:
3322:
3320:
3317:
3315:
3312:
3310:
3309:Oxyanion hole
3307:
3305:
3302:
3300:
3297:
3295:
3292:
3291:
3289:
3285:
3281:
3274:
3269:
3267:
3262:
3260:
3255:
3254:
3251:
3239:
3236:
3232:
3229:
3227:
3224:
3223:
3222:
3219:
3217:
3214:
3212:
3209:
3207:
3204:
3202:
3199:
3197:
3194:
3192:
3189:
3187:
3184:
3180:
3177:
3175:
3172:
3170:
3167:
3165:
3162:
3160:
3157:
3155:
3152:
3151:
3150:
3147:
3145:
3142:
3141:
3139:
3136:
3132:
3126:
3123:
3121:
3118:
3116:
3113:
3112:
3110:
3107:
3103:
3095:
3092:
3090:
3087:
3085:
3082:
3080:
3077:
3075:
3072:
3070:
3067:
3065:
3064:Phenylalanine
3062:
3060:
3057:
3055:
3052:
3050:
3047:
3045:
3042:
3040:
3037:
3035:
3032:
3030:
3027:
3025:
3022:
3020:
3017:
3015:
3012:
3010:
3007:
3005:
3002:
3000:
2997:
2995:
2992:
2991:
2990:
2987:
2986:
2984:
2981:
2977:
2972:
2968:
2964:
2957:
2952:
2950:
2945:
2943:
2938:
2937:
2934:
2924:
2923:
2916:
2906:
2903:
2901:
2898:
2896:
2893:
2891:
2888:
2886:
2883:
2881:
2878:
2876:
2873:
2871:
2868:
2866:
2863:
2861:
2858:
2856:
2853:
2851:
2848:
2846:
2843:
2841:
2838:
2836:
2833:
2831:
2828:
2826:
2823:
2821:
2818:
2816:
2813:
2811:
2808:
2806:
2803:
2801:
2798:
2797:
2795:
2792:
2787:
2781:
2778:
2776:
2773:
2772:
2770:
2767:
2762:
2756:
2753:
2751:
2748:
2746:
2743:
2742:
2740:
2737:
2732:
2726:
2723:
2722:
2720:
2717:
2712:
2706:
2703:
2701:
2698:
2696:
2693:
2691:
2688:
2686:
2683:
2681:
2678:
2676:
2673:
2672:
2670:
2667:
2662:
2659:
2657:
2653:
2643:
2640:
2636:
2633:
2631:
2628:
2627:
2626:
2623:
2621:
2618:
2617:
2614:
2611:
2607:
2597:
2594:
2593:
2590:
2584:
2581:
2580:
2578:
2575:
2570:
2564:
2561:
2559:
2556:
2554:
2551:
2550:
2548:
2545:
2544:
2538:
2532:
2529:
2527:
2524:
2522:
2519:
2518:
2516:
2513:
2512:
2506:
2500:
2497:
2495:
2492:
2490:
2487:
2485:
2482:
2480:
2477:
2475:
2472:
2470:
2467:
2466:
2464:
2461:
2460:
2454:
2451:
2449:
2445:
2435:
2432:
2430:
2427:
2425:
2422:
2420:
2417:
2415:
2412:
2411:
2409:
2406:
2401:
2395:
2392:
2390:
2387:
2385:
2382:
2381:
2379:
2376:
2375:
2369:
2363:
2360:
2358:
2355:
2354:
2352:
2349:
2348:
2342:
2336:
2333:
2332:
2330:
2327:
2326:
2320:
2314:
2311:
2309:
2306:
2304:
2301:
2299:
2296:
2295:
2293:
2290:
2289:
2283:
2280:
2278:
2274:
2268:
2265:
2263:
2260:
2259:
2257:
2255:
2251:
2241:
2238:
2237:
2235:
2232:
2229:
2223:
2217:
2214:
2213:
2211:
2208:
2206:
2200:
2194:
2191:
2189:
2186:
2185:
2183:
2180:
2179:
2173:
2170:
2168:
2164:
2159:
2158:Mitochondrial
2152:
2147:
2145:
2140:
2138:
2133:
2132:
2129:
2113:
2110:
2108:
2105:
2104:
2102:
2098:
2092:
2089:
2087:
2084:
2082:
2079:
2077:
2074:
2072:
2069:
2067:
2064:
2062:
2059:
2057:
2054:
2052:
2049:
2047:
2044:
2042:
2038:
2032:
2031:
2028:
2025:
2023:
2020:
2018:
2015:
2013:
2006:
2004:
2001:
1999:
1996:
1995:
1993:
1989:
1986:
1984:
1979:
1975:Mitochondrial
1973:
1963:
1960:
1958:
1955:
1954:
1952:
1950:
1945:
1939:
1936:
1935:
1933:
1931:
1926:
1920:
1917:
1916:
1914:
1912:
1907:
1900:
1896:
1892:
1891:
1887:
1883:
1879:
1875:
1872:
1871:
1869:
1867:
1862:
1859:
1857:
1853:
1846:
1843:
1841:
1838:
1835:
1831:
1828:
1827:
1824:
1821:
1819:
1816:
1814:
1811:
1809:
1806:
1804:
1801:
1800:
1798:
1794:
1790:
1787:
1783:
1776:
1771:
1769:
1764:
1762:
1757:
1756:
1753:
1746:
1742:
1739:
1738:
1734:
1725:
1721:
1716:
1711:
1707:
1703:
1699:
1695:
1691:
1684:
1682:
1678:
1673:
1669:
1665:
1661:
1657:
1653:
1646:
1643:
1638:
1634:
1630:
1626:
1622:
1618:
1611:
1608:
1603:
1599:
1596:(3): 117–25.
1595:
1591:
1584:
1581:
1576:
1572:
1568:
1564:
1559:
1554:
1550:
1546:
1542:
1535:
1532:
1527:
1523:
1519:
1515:
1512:(4): 401–10.
1511:
1507:
1500:
1497:
1492:
1488:
1484:
1480:
1477:(2): 403–15.
1476:
1472:
1465:
1462:
1457:
1453:
1448:
1443:
1439:
1435:
1431:
1424:
1421:
1416:
1412:
1407:
1402:
1398:
1394:
1390:
1383:
1381:
1377:
1372:
1368:
1363:
1358:
1354:
1350:
1346:
1339:
1337:
1335:
1333:
1329:
1324:
1320:
1316:
1312:
1309:(2): 537–46.
1308:
1304:
1296:
1294:
1290:
1285:
1281:
1277:
1273:
1269:
1265:
1258:
1256:
1252:
1247:
1243:
1238:
1233:
1229:
1225:
1221:
1214:
1212:
1210:
1206:
1201:
1197:
1193:
1189:
1185:
1181:
1173:
1171:
1169:
1165:
1160:
1156:
1152:
1150:9780470123041
1146:
1142:
1138:
1134:
1127:
1124:
1119:
1117:0-7167-3051-0
1113:
1109:
1104:
1103:
1094:
1092:
1090:
1086:
1081:
1075:
1071:
1064:
1062:
1058:
1053:
1049:
1045:
1041:
1037:
1033:
1026:
1023:
1018:
1014:
1009:
1004:
1000:
996:
992:
985:
982:
975:
971:
968:
966:
963:
961:
958:
956:
953:
952:
948:
942:
937:
932:
930:
928:
924:
920:
916:
913:
909:
905:
898:
896:
890:
888:
886:
882:
878:
875:
871:
867:
863:
859:
851:
849:
847:
844:
840:
836:
832:
828:
820:
818:
816:
812:
807:
802:
798:
790:
785:
783:
777:
771:
769:
765:
761:
757:
753:
749:
742:
738:
735:
732:
730:
726:
723:
720:
719:
718:
716:
708:
706:
703:
699:
695:
690:
686:
682:
681:Rossmann fold
678:
674:
666:
664:
662:
659:
655:
631:
627:
623:
619:
616:
612:
608:
597:
593:
592:
587:
579:
574:
572:
570:
565:
562:
558:
554:
550:
546:
537:
536:
535:
533:
525:
523:
521:
517:
513:
509:
505:
501:
497:
493:
489:
485:
481:
477:
473:
469:
465:
461:
457:
445:
442:
440:
436:
433:
430:
428:
424:
421:
418:
416:
412:
407:
403:
400:
396:
393:
391:
390:Gene Ontology
387:
384:
381:
378:
375:
372:
368:
365:
362:
360:
356:
353:
350:
348:
344:
341:
338:
336:
332:
329:
328:NiceZyme view
326:
324:
320:
317:
314:
312:
308:
305:
302:
300:
296:
291:
288:
285:
283:
279:
276:
273:
271:
267:
262:
257:
252:
246:
241:
236:
225:
222:
220:
216:
213:
210:
208:
204:
201:
198:
196:
192:
187:
183:
180:
176:
173:
171:
170:Gene Ontology
167:
164:
161:
158:
155:
152:
148:
145:
142:
140:
136:
133:
130:
128:
124:
121:
118:
116:
112:
109:
108:NiceZyme view
106:
104:
100:
97:
94:
92:
88:
85:
82:
80:
76:
71:
68:
65:
63:
59:
56:
53:
51:
47:
42:
37:
30:
25:
20:
3523:Translocases
3520:
3507:
3494:
3481:
3468:
3458:Transferases
3455:
3442:
3299:Binding site
3211:GMP synthase
3114:
2919:
2766:ATP synthase
2573:
2541:
2509:
2488:
2457:
2424:ATP synthase
2404:
2372:
2345:
2323:
2303:Cytochrome c
2286:
2226:
2216:Kynureninase
2203:
2176:
2033:
2022:Cytochrome c
1930:succinyl-CoA
1822:
1700:(2): 383–7.
1697:
1693:
1658:(1): 245–9.
1655:
1651:
1645:
1620:
1616:
1610:
1593:
1589:
1583:
1551:(2): 215–8.
1548:
1545:FEBS Letters
1544:
1534:
1509:
1505:
1499:
1474:
1470:
1464:
1437:
1433:
1423:
1396:
1392:
1352:
1348:
1306:
1303:Biochemistry
1302:
1270:(1): 17–25.
1267:
1264:Biochemistry
1263:
1227:
1223:
1183:
1180:Biochemistry
1179:
1132:
1126:
1101:
1069:
1035:
1031:
1025:
998:
994:
984:
903:
902:
894:
855:
846:biosynthesis
824:
800:
794:
772:
745:
712:
694:conformation
672:
670:
651:
629:
625:
615:crystallized
610:
596:heterodimers
589:
583:
566:
557:nucleophilic
541:
529:
480:succinyl-CoA
471:
467:
463:
459:
455:
454:
316:BRENDA entry
250:
96:BRENDA entry
3294:Active site
2716:Complex III
2039:synthesis:
1856:Anaplerotic
1623:(1): 53–9.
1102:Biochemistr
862:transcribed
843:ketone body
748:heterodimer
698:Mutagenesis
660:code 1CQJ.
545:free energy
522:of a cell.
304:IntEnz view
264:Identifiers
84:IntEnz view
44:Identifiers
3550:Metabolism
3544:Categories
3497:Isomerases
3471:Hydrolases
3338:Regulation
3084:Tryptophan
3059:Methionine
3044:Isoleucine
3004:Asparagine
2736:Complex IV
2543:urea cycle
2231:metabolism
2207:metabolism
2205:tryptophan
2034:Coenzyme Q
2008:Coenzyme Q
1866:acetyl-CoA
1782:Metabolism
1230:(3): 501.
976:References
923:glycolysis
885:inhibitors
689:N-terminus
498:) from an
373:structures
340:KEGG entry
287:9080-33-5
153:structures
120:KEGG entry
67:9014-36-2
3376:EC number
3079:Threonine
3039:Histidine
3029:Glutamine
3024:Glutamate
3009:Aspartate
2920:see also
2666:Complex I
2474:Aconitase
1808:Aconitase
912:base pair
858:regulated
835:porphyrin
756:guanosine
752:adenosine
702:glutamate
685:ATP grasp
575:Structure
561:histidine
549:mechanism
484:succinate
476:catalyzes
293:Databases
73:Databases
3555:EC 6.2.1
3400:Kinetics
3324:Cofactor
3287:Activity
3089:Tyrosine
3014:Cysteine
2999:Arginine
2973:6.1-6.3)
2620:Frataxin
2494:Fumarase
2160:proteins
1840:Fumarase
1724:17668387
1637:10376993
1575:23667115
1415:15234968
1323:11781092
1284:10625475
1246:10329157
1017:16481318
933:See also
915:deletion
870:promoter
786:Function
715:amniotes
709:Isoforms
626:Image 2:
586:subunits
580:Subunits
444:proteins
432:articles
420:articles
377:RCSB PDB
224:proteins
212:articles
200:articles
157:RCSB PDB
3510:Ligases
3280:Enzymes
3069:Proline
3049:Leucine
3034:Glycine
2994:Alanine
2967:ligases
2963:Enzymes
2780:MT-ATP8
2775:MT-ATP6
2695:MT-ND4L
2012:(CoQ10)
1991:Primary
1847:and ETC
1789:enzymes
1715:1950792
1567:2943604
1526:6263728
1491:5879477
1456:9765290
1371:9765291
1200:3535876
1159:3521216
1052:9917402
801:E. coli
737:6.2.1.4
725:6.2.1.5
673:E. coli
630:E. coli
611:E. coli
594:two αβ
591:E. coli
399:QuickGO
364:profile
347:MetaCyc
282:CAS no.
275:6.2.1.5
179:QuickGO
144:profile
127:MetaCyc
62:CAS no.
55:6.2.1.4
3484:Lyases
3154:Cullin
3094:Valine
3074:Serine
3054:Lysine
2885:MT-TS2
2880:MT-TS1
2850:MT-TL2
2845:MT-TL1
2755:MT-CO3
2750:MT-CO2
2745:MT-CO1
2725:MT-CYB
2705:MT-ND6
2700:MT-ND5
2690:MT-ND4
2685:MT-ND3
2680:MT-ND2
2675:MT-ND1
2448:Matrix
2081:COQ10B
2076:COQ10A
1747:(MeSH)
1722:
1712:
1672:564714
1670:
1635:
1602:179232
1600:
1573:
1565:
1524:
1489:
1454:
1413:
1369:
1321:
1282:
1244:
1198:
1157:
1147:
1114:
1110:–477.
1076:
1050:
1015:
919:SUCLG1
877:operon
841:, and
806:pigeon
760:SUCLG1
741:SUCLG2
729:SUCLA2
642:yellow
588:. In
427:PubMed
409:Search
395:AmiGO
383:PDBsum
323:ExPASy
311:BRENDA
299:IntEnz
270:EC no.
253:. PDB
207:PubMed
189:Search
175:AmiGO
163:PDBsum
103:ExPASy
91:BRENDA
79:IntEnz
50:EC no.
3436:Types
3164:UBE3A
2905:MT-TY
2900:MT-TW
2895:MT-TV
2890:MT-TT
2875:MT-TR
2870:MT-TQ
2865:MT-TP
2860:MT-TN
2855:MT-TM
2840:MT-TK
2835:MT-TI
2830:MT-TH
2825:MT-TG
2820:MT-TF
2815:MT-TE
2810:MT-TD
2805:MT-TC
2800:MT-TA
2596:PMPCB
2583:ALDH2
2405:other
2100:Other
2091:PDSS2
2086:PDSS1
1796:Cycle
1571:S2CID
677:binds
638:green
359:PRIAM
139:PRIAM
3528:list
3521:EC7
3515:list
3508:EC6
3502:list
3495:EC5
3489:list
3482:EC4
3476:list
3469:EC3
3463:list
3456:EC2
3450:list
3443:EC1
3179:UBR1
3169:Mdm2
2791:tRNA
2071:COQ9
2066:COQ7
2061:COQ6
2056:COQ5
2051:COQ4
2046:COQ3
2041:COQ2
1897:and
1834:SDHA
1720:PMID
1668:PMID
1633:PMID
1598:PMID
1563:PMID
1522:PMID
1487:PMID
1452:PMID
1411:PMID
1367:PMID
1319:PMID
1280:PMID
1242:PMID
1196:PMID
1155:PMID
1145:ISBN
1112:ISBN
1074:ISBN
1048:PMID
1013:PMID
839:heme
827:flux
652:The
646:blue
644:and
636:and
634:pink
628:The
439:NCBI
380:PDBe
335:KEGG
256:2scu
219:NCBI
160:PDBe
115:KEGG
36:2fp4
3135:6.3
3106:6.2
2980:6.1
1947:to
1928:to
1909:to
1864:to
1710:PMC
1702:doi
1660:doi
1656:523
1625:doi
1621:100
1553:doi
1549:205
1514:doi
1479:doi
1475:111
1442:doi
1438:273
1401:doi
1397:279
1357:doi
1353:273
1311:doi
1272:doi
1232:doi
1228:288
1188:doi
1137:doi
1108:475
1040:doi
1036:285
1003:doi
999:281
768:ATP
766:or
764:GTP
754:or
658:PDB
553:CoA
508:ADP
506:or
504:GDP
496:ATP
494:or
492:GTP
482:to
470:or
466:or
460:SCS
415:PMC
371:PDB
195:PMC
151:PDB
3546::
3231:II
2971:EC
2036:10
2010:10
1886:E3
1884:,
1882:E2
1880:,
1878:E1
1784::
1718:.
1708:.
1698:81
1696:.
1692:.
1680:^
1666:.
1654:.
1631:.
1619:.
1594:50
1592:.
1569:.
1561:.
1547:.
1543:.
1520:.
1510:13
1508:.
1485:.
1473:.
1450:.
1436:.
1432:.
1409:.
1395:.
1391:.
1379:^
1365:.
1351:.
1347:.
1331:^
1317:.
1307:41
1305:.
1292:^
1278:.
1268:39
1266:.
1254:^
1240:.
1226:.
1222:.
1208:^
1194:.
1184:25
1182:.
1167:^
1153:.
1143:.
1088:^
1060:^
1046:.
1034:.
1011:.
997:.
993:.
848:.
837:,
734:EC
722:EC
663:.
534::
397:/
177:/
3530:)
3526:(
3517:)
3513:(
3504:)
3500:(
3491:)
3487:(
3478:)
3474:(
3465:)
3461:(
3452:)
3448:(
3272:e
3265:t
3258:v
3226:I
2969:(
2955:e
2948:t
2941:v
2150:e
2143:t
2136:v
1980:/
1901:)
1888:)
1876:(
1836:)
1832:(
1774:e
1767:t
1760:v
1726:.
1704::
1674:.
1662::
1639:.
1627::
1604:.
1577:.
1555::
1528:.
1516::
1493:.
1481::
1458:.
1444::
1417:.
1403::
1373:.
1359::
1325:.
1313::
1286:.
1274::
1248:.
1234::
1202:.
1190::
1161:.
1139::
1120:.
1082:.
1054:.
1042::
1019:.
1005::
780:m
604:2
602:β
600:2
458:(
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.
