Knowledge (XXG)

Triosephosphate isomerase

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The structure of triose phosphate isomerase contributes to its function. Besides the precisely placed glutamate and histidine residues to form the enediol, a ten- or eleven-amino acid chain of TPI acts as a loop to stabilize the intermediate. The loop, formed by residues 166 to 176, closes and
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Studies suggest that a lysine close to the active site (at position 12) is also crucial for enzyme function. The lysine, protonated at physiological pH, may help neutralize the negative charge of the phosphate group. When this lysine residue is replaced with a neutral amino acid, TPI loses all
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histidine 95 residue donates a proton to form the enediol intermediate. When deprotonated, the enediolate then collapses and, abstracting a proton from protonated glutamate 165, forms the GAP product. Catalysis of the reverse reaction proceeds analogously, forming the same enediol but with
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TPI is diffusion-limited. In terms of thermodynamics, DHAP formation is favored 20:1 over GAP production. However, in glycolysis, the use of GAP in the subsequent steps of metabolism drives the reaction toward its production. TPI is inhibited by
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and inorganic phosphate. The hydrogen bond between the enzyme and the phosphate group of the substrate makes such decomposition stereoelectronically unfavorable. Methylglyoxal is a toxin and, if formed, is removed through the
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Nickbarg EB, Davenport RC, Petsko GA, Knowles JR (August 1988). "Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism".
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Triose phosphate isomerase is a highly efficient enzyme, performing the reaction billions of times faster than it would occur naturally in solution. The reaction is so efficient that it is said to be
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Lolis E, Petsko GA (July 1990). "Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis".
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on the inside. In the illustration, the ribbon backbone of each subunit is colored in blue to red from N-terminus to C-terminus. This structural motif is called an ιβ-barrel, or a
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Komives EA, Chang LC, Lolis E, Tilton RF, Petsko GA, Knowles JR (March 1991). "Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95".
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Creighton DJ, Hamilton DS (March 2001). "Brief history of glyoxalase I and what we have learned about metal ion-dependent, enzyme-catalyzed isomerizations".
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Lodi PJ, Chang LC, Knowles JR, Komives EA (March 1994). "Triosephosphate isomerase requires a positively charged active site: the role of lysine-12".
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and is essential for efficient energy production. TPI has been found in nearly every organism searched for the enzyme, including animals such as
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In addition to making the reaction kinetically feasible, the TPI loop sequesters the reactive enediol intermediate to prevent decomposition to
775: 605: 434: 1293: 468:. The relative free energy of each ground state and transition state has been determined experimentally, and is displayed in the figure. 1119:"Kinetic properties of triose-phosphate isomerase from Trypanosoma brucei brucei. A comparison with the rabbit muscle and yeast enzymes" 757:. The loss of a high-energy phosphate bond and the substrate for the rest of glycolysis makes formation of methylglyoxal inefficient. 478:
The structure of TPI facilitates the conversion between dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (GAP). The
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Harris TK, Cole RN, Comer FI, Mildvan AS (November 1998). "Proton transfer in the mechanism of triosephosphate isomerase".
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Albery WJ, Knowles JR (December 1976). "Free-energy profile of the reaction catalyzed by triosephosphate isomerase".
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provides an overview of all the structure information available in the PDB for Human Triosephosphate isomerase
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that cause this disease, most include the replacement of glutamic acid at position 104 with an aspartic acid.
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Rose IA, Fung WJ, Warms JV (May 1990). "Proton diffusion in the active site of triosephosphate isomerase".
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to the phosphate group of the substrate. This action stabilizes the enediol intermediate and the other
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In humans, deficiencies in TPI are associated with a progressive, severe neurological disorder called
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function, but variants with a different positively charged amino acid retain some function.
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Alber T, Banner DW, Bloomer AC, Petsko GA, Phillips D, Rivers PS, Wilson IA (June 1981).
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Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
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Knowles JR (March 1991). "Enzyme catalysis: not different, just better".
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residues. The three-dimensional structure of a subunit contains eight
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Side view of triose P isomerase monomer, active site at top center
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The mechanism involves the intermediate formation of an
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Lambeir AM, Opperdoes FR, Wierenga RK (October 1987).
2753: 452:: It is limited only by the rate the substrate can 2649: 2613: 2582: 2551: 2500: 2422: 2398: 2314: 2278: 2237: 2148: 2119: 2095: 2071: 2046: 2039: 1894: 671: 651: 633: 628: 604: 592: 580: 567: 555: 547: 542: 537: 223: 211: 199: 194: 174: 155: 143: 131: 119: 107: 95: 83: 78: 66: 54: 49: 32: 1042: 1040: 1038: 511:. Other inhibitors include 2-phosphoglycolate, a 2156:Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase 721:of this enzyme is in the center of the barrel. A 526:Side view of triose phosphate isomerase dimer. 482:glutamate 165 residue of TPI deprotonates the 2478: 2375:5-carboxymethyl-2-hydroxymuconate D-isomerase 2206: 1857: 1287: 8: 713:, and is by far the most commonly observed 491:enediolate collapse from the oxygen at C2. 2485: 2471: 2463: 2213: 2199: 2191: 2043: 1898: 1864: 1850: 1842: 1294: 1280: 1272: 817:Orosz F, OlĂĄh J, OvĂĄdi J (December 2006). 625: 456:into and out of the enzyme's active site. 191: 38: 1134: 948: 834: 1998:Glyceraldehyde 3-phosphate dehydrogenase 856: 854: 697:, each of which is made up of about 250 2760: 2330:Isopentenyl-diphosphate delta isomerase 1195:Archives of Biochemistry and Biophysics 809: 795:Triosephosphate isomerase (TIM) family 534: 333: 292: 267:the reversible interconversion of the 29: 776:Triose Phosphate Isomerase deficiency 435:triose phosphate isomerase deficiency 7: 356: 348: 315: 1136:10.1111/j.1432-1033.1987.tb13388.x 705:on the outside and eight parallel 25: 2063:Phosphoenolpyruvate carboxykinase 2763: 2370:Prostaglandin-A1 Delta-isomerase 1827: 1804: 1779: 1744: 1708: 1685: 1668: 1637: 1612: 1578: 1548: 1525: 1506: 1480: 1463: 1444: 1427: 1402: 1385: 1366: 1349: 1324: 1123:European Journal of Biochemistry 689:Triose phosphate isomerase is a 515:, and D-glycerol-1-phosphate, a 471: 334: 319: 309: 402:TPI plays an important role in 2390:Polyenoic fatty acid isomerase 1967:Fructose-bisphosphate aldolase 1: 629:Available protein structures: 27:Enzyme involved in glycolysis 2306:4-Oxalocrotonate tautomerase 2260:Ribose-5-phosphate isomerase 2409:Protein disulfide-isomerase 2380:Isopiperitenone D-isomerase 2355:Methylitaconate D-isomerase 2345:Cholestenol Delta-isomerase 2335:Vinylacetyl-CoA D-isomerase 2265:Mannose phosphate isomerase 1953:Fructose 1,6-bisphosphatase 441:. While there are various 2812: 2296:Phenylpyruvate tautomerase 2180:Bisphosphoglycerate mutase 1559:Glyceraldehyde-3-phosphate 1540:Glyceraldehyde 3-phosphate 1501:Glyceraldehyde 3-phosphate 1475:Dihydroxyacetone phosphate 358:triose phosphate isomerase 344: 342: 329: 327: 303:glyceraldehyde 3-phosphate 294:triose phosphate isomerase 289:Dihydroxyacetone phosphate 280:glyceraldehyde 3-phosphate 276:dihydroxyacetone phosphate 242:Triose-phosphate isomerase 2641:Michaelis–Menten kinetics 2433:Prostaglandin D2 synthase 2360:Aconitate Delta-isomerase 2340:Muconolactone D-isomerase 2255:Triosephosphate isomerase 1993: 1985:Triosephosphate isomerase 1962: 1901: 1439:Fructose 1,6-bisphosphate 1312: 836:10.1080/15216540601115960 786:Triosephosphate isomerase 745:on the reaction pathway. 624: 538:Triosephosphate isomerase 318: 308: 190: 37: 33:triosephosphate isomerase 2533:Diffusion-limited enzyme 2442:Prostaglandin E synthase 2437:Prostaglandin-D synthase 2301:Oxaloacetate tautomerase 507:ions, which bind to the 18:Triosephosphateisomerase 2008:Phosphoglycerate mutase 2003:Phosphoglycerate kinase 1877:carbohydrate metabolism 1679:Phosphoglycerate mutase 1623:Phosphoglycerate kinase 1604:1,3-Bisphosphoglycerate 513:transition state analog 2452:Thromboxane-A synthase 2385:L-dopachrome isomerase 2136:Glycerol dehydrogenase 1207:10.1006/abbi.2000.2253 950:10.1098/rstb.1981.0069 527: 2626:Eadie–Hofstee diagram 2559:Allosteric regulation 2447:Prostacyclin synthase 2087:Lactate dehydrogenase 1937:Phosphofructokinase 1 1926:Glucose 6-phosphatase 1455:Fructose-bisphosphate 1413:Phosphofructokinase-1 788:in interactive 3D at 525: 450:catalytically perfect 2636:Lineweaver–Burk plot 2111:Alanine transaminase 2058:Pyruvate carboxylase 2040:Gluconeogenesis only 1397:Fructose 6-phosphate 729:are involved in the 2365:Enoyl CoA isomerase 2325:Steroid D-isomerase 1771:Phosphoenolpyruvate 1377:Glucose-6-phosphate 1361:Glucose 6-phosphate 1242:10.1021/bi00176a009 1172:10.1021/bi00480a010 1021:10.1021/bi00226a005 986:10.1021/bi00416a019 910:10.1021/bi00470a008 875:10.1021/bi00670a031 731:catalytic mechanism 2791:Glycolysis enzymes 2595:Enzyme superfamily 2528:Enzyme promiscuity 1826: 1817: 1778: 1769: 1707: 1700:2-Phosphoglycerate 1698: 1667: 1660:3-Phosphoglycerate 1658: 1611: 1602: 1547: 1538: 528: 2751: 2750: 2460: 2459: 2270:Glucose isomerase 2224:: intramolecular 2188: 2187: 2144: 2143: 2035: 2034: 1932:Glucose isomerase 1839: 1838: 1824: 1815: 1776: 1767: 1705: 1696: 1665: 1656: 1609: 1600: 1545: 1536: 1306:metabolic pathway 1096:10.1021/bi982089f 755:glyoxalase system 743:transition states 687: 686: 683: 682: 678:structure summary 398:Pathway Database. 387:Pathway Database. 376:Pathway Database. 365: 364: 300: 239: 238: 235: 234: 138:metabolic pathway 16:(Redirected from 2803: 2768: 2767: 2759: 2631:Hanes–Woolf plot 2574:Enzyme activator 2569:Enzyme inhibitor 2543:Enzyme catalysis 2487: 2480: 2473: 2464: 2215: 2208: 2201: 2192: 2044: 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1835: 1834: 1833: 1832: 1822: 1811: 1810: 1809: 1801: 1800: 1797: 1793: 1790:Pyruvate kinase 1785: 1784: 1774: 1763: 1762: 1761: 1759: 1754: 1750: 1749: 1741: 1740: 1738: 1733: 1729: 1720: 1719:Phosphopyruvate 1714: 1713: 1703: 1692: 1691: 1690: 1682: 1674: 1673: 1663: 1652: 1651: 1650: 1647: 1643: 1642: 1634: 1633: 1630: 1626: 1618: 1617: 1607: 1596: 1595: 1594: 1591: 1590: 1584: 1583: 1575: 1574: 1571: 1570: 1564: 1560: 1554: 1553: 1543: 1532: 1531: 1530: 1522: 1518: 1517:Triosephosphate 1512: 1511: 1504: 1496: 1495: 1492: 1486: 1485: 1478: 1470: 1469: 1468: 1460: 1456: 1450: 1449: 1442: 1434: 1433: 1432: 1424: 1423: 1420: 1416: 1408: 1407: 1400: 1392: 1391: 1390: 1382: 1378: 1372: 1371: 1364: 1356: 1355: 1354: 1346: 1345: 1342: 1338: 1330: 1329: 1322: 1308: 1300: 1262: 1257: 1236:(10): 2809–14. 1227: 1226: 1222: 1192: 1191: 1187: 1166:(28): 6619–25. 1157: 1156: 1152: 1116: 1115: 1111: 1081: 1080: 1076: 1055:(6314): 121–4. 1046: 1045: 1036: 1006: 1005: 1001: 980:(16): 5948–60. 971: 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13: 10: 9: 6: 4: 3: 2: 2808: 2797: 2794: 2792: 2789: 2787: 2784: 2783: 2781: 2771: 2766: 2761: 2757: 2743: 2739: 2738: 2733: 2730: 2726: 2725: 2720: 2717: 2713: 2712: 2707: 2704: 2700: 2699: 2694: 2691: 2687: 2686: 2681: 2678: 2674: 2673: 2668: 2665: 2661: 2660: 2655: 2654: 2652: 2648: 2642: 2639: 2637: 2634: 2632: 2629: 2627: 2624: 2622: 2619: 2618: 2616: 2612: 2606: 2603: 2601: 2600:Enzyme family 2598: 2596: 2593: 2591: 2588: 2587: 2585: 2581: 2575: 2572: 2570: 2567: 2565: 2564:Cooperativity 2562: 2560: 2557: 2556: 2554: 2550: 2544: 2541: 2539: 2536: 2534: 2531: 2529: 2526: 2524: 2523:Oxyanion hole 2521: 2519: 2516: 2514: 2511: 2509: 2506: 2505: 2503: 2499: 2495: 2488: 2483: 2481: 2476: 2474: 2469: 2468: 2465: 2453: 2450: 2448: 2445: 2443: 2440: 2438: 2434: 2431: 2430: 2428: 2425: 2421: 2414: 2410: 2407: 2406: 2404: 2401: 2397: 2391: 2388: 2386: 2383: 2381: 2378: 2376: 2373: 2371: 2368: 2366: 2363: 2361: 2358: 2356: 2353: 2350: 2346: 2343: 2341: 2338: 2336: 2333: 2331: 2328: 2326: 2323: 2322: 2320: 2317: 2313: 2307: 2304: 2302: 2299: 2297: 2294: 2293: 2291: 2289: 2285: 2281: 2277: 2271: 2268: 2266: 2263: 2261: 2258: 2256: 2253: 2252: 2250: 2248: 2244: 2240: 2236: 2231: 2227: 2223: 2216: 2211: 2209: 2204: 2202: 2197: 2196: 2193: 2181: 2178: 2174: 2170: 2166: 2162: 2159: 2158: 2157: 2154: 2153: 2151: 2147: 2137: 2134: 2132: 2129: 2128: 2126: 2123: 2118: 2112: 2109: 2108: 2106: 2103: 2102:Alanine cycle 2099: 2094: 2088: 2085: 2084: 2082: 2079: 2075: 2070: 2064: 2061: 2059: 2056: 2055: 2053: 2050: 2045: 2042: 2038: 2027: 2023: 2019: 2016: 2014: 2011: 2009: 2006: 2004: 2001: 1999: 1996: 1995: 1992: 1986: 1983: 1980: 1976: 1972: 1968: 1965: 1964: 1961: 1954: 1950: 1946: 1942: 1938: 1935: 1933: 1930: 1927: 1923: 1919: 1915: 1911: 1907: 1904: 1903: 1900: 1897: 1893: 1889: 1886: 1882: 1878: 1874: 1867: 1862: 1860: 1855: 1853: 1848: 1847: 1844: 1830: 1821: 1820: 1807: 1792: 1791: 1782: 1773: 1772: 1747: 1728: 1726: 1722: 1711: 1702: 1701: 1688: 1681: 1680: 1671: 1662: 1661: 1640: 1625: 1624: 1615: 1606: 1605: 1581: 1563: 1562: 1561:dehydrogenase 1551: 1542: 1541: 1528: 1521: 1520: 1509: 1503: 1502: 1491: 1483: 1477: 1476: 1466: 1459: 1458: 1447: 1441: 1440: 1430: 1415: 1414: 1405: 1399: 1398: 1388: 1381: 1380: 1369: 1363: 1362: 1352: 1337: 1336: 1327: 1321: 1320: 1311: 1307: 1304: 1297: 1292: 1290: 1285: 1283: 1278: 1277: 1274: 1267: 1264: 1263: 1259: 1251: 1247: 1243: 1239: 1235: 1231: 1224: 1221: 1216: 1212: 1208: 1204: 1200: 1196: 1189: 1186: 1181: 1177: 1173: 1169: 1165: 1161: 1154: 1151: 1146: 1142: 1137: 1132: 1128: 1124: 1120: 1113: 1110: 1105: 1101: 1097: 1093: 1089: 1085: 1078: 1075: 1070: 1066: 1062: 1058: 1054: 1050: 1043: 1041: 1039: 1035: 1030: 1026: 1022: 1018: 1014: 1010: 1003: 1000: 995: 991: 987: 983: 979: 975: 968: 965: 960: 956: 951: 946: 942: 938: 934: 927: 924: 919: 915: 911: 907: 903: 899: 892: 889: 884: 880: 876: 872: 868: 864: 857: 855: 851: 846: 842: 837: 832: 828: 824: 820: 813: 810: 804: 800: 796: 793: 791: 787: 784: 782: 779: 777: 774: 772: 769: 768: 764: 762: 758: 756: 751: 750:methylglyoxal 746: 744: 740: 739:hydrogen bond 734: 732: 728: 724: 723:glutamic acid 720: 716: 712: 708: 704: 700: 696: 693:of identical 692: 679: 676: 674: 670: 667: 663: 659: 656: 654: 650: 646: 642: 639: 636: 632: 627: 623: 620: 616: 612: 609: 607: 603: 600: 597: 595: 591: 588: 585: 583: 579: 576: 573: 570: 566: 563: 560: 558: 554: 550: 546: 541: 536: 530: 524: 520: 518: 514: 510: 506: 502: 498: 492: 489: 488:electrophilic 485: 481: 476: 474: 469: 467: 459: 457: 455: 451: 446: 444: 440: 436: 431: 429: 425: 421: 417: 413: 409: 405: 400: 397: 393: 386: 382: 375: 371: 361: 359: 353: 352: 347: 341: 337: 332: 326: 322: 312: 307: 304: 297: 295: 290: 287: 286: 283: 281: 277: 274: 270: 266: 262: 259: 255: 251: 247: 243: 231: 228: 226: 222: 219: 216: 214: 210: 207: 204: 202: 198: 193: 189: 186: 182: 179: 177: 176:Gene Ontology 173: 170: 167: 164: 161: 158: 154: 151: 148: 146: 142: 139: 136: 134: 130: 127: 124: 122: 118: 115: 114:NiceZyme view 112: 110: 106: 103: 100: 98: 94: 91: 88: 86: 82: 77: 74: 71: 69: 65: 62: 59: 57: 53: 48: 41: 36: 31: 19: 2737:Translocases 2734: 2721: 2708: 2695: 2682: 2672:Transferases 2669: 2656: 2513:Binding site 2254: 2049:oxaloacetate 1984: 1814: 1788: 1766: 1717: 1695: 1677: 1655: 1621: 1599: 1557: 1535: 1516: 1515: 1499: 1489: 1473: 1453: 1437: 1411: 1395: 1375: 1359: 1333: 1317: 1233: 1230:Biochemistry 1229: 1223: 1198: 1194: 1188: 1163: 1160:Biochemistry 1159: 1153: 1129:(1): 69–74. 1126: 1122: 1112: 1087: 1084:Biochemistry 1083: 1077: 1052: 1048: 1012: 1009:Biochemistry 1008: 1002: 977: 974:Biochemistry 973: 967: 940: 936: 926: 901: 898:Biochemistry 897: 891: 866: 863:Biochemistry 862: 826: 822: 812: 759: 747: 735: 715:protein fold 688: 493: 480:nucleophilic 477: 470: 463: 447: 432: 430:, lack TPI. 401: 366: 249: 245: 241: 240: 102:BRENDA entry 2508:Active site 1922:Glucokinase 1201:(1): 1–10. 790:Proteopedia 719:active site 543:Identifiers 509:active site 428:ureaplasmas 90:IntEnz view 50:Identifiers 2796:Glycolysis 2780:Categories 2711:Isomerases 2685:Hydrolases 2552:Regulation 2222:Isomerases 2149:Regulatory 2078:Cori cycle 1969:(Aldolase 1906:Hexokinase 1895:Glycolysis 1881:glycolysis 1873:Metabolism 1335:Hexokinase 1303:Glycolysis 823:IUBMB Life 805:References 771:TIM barrel 711:TIM-barrel 699:amino acid 641:structures 486:, and the 404:glycolysis 271:phosphate 159:structures 126:KEGG entry 73:9023-78-3 2590:EC number 1721:hydratase 1519:isomerase 1379:isomerase 727:histidine 707:β-strands 703:Îą-helices 599:PDOC00155 587:IPR000652 531:Structure 501:phosphate 484:substrate 460:Mechanism 443:mutations 390:Compound 368:Compound 265:catalyzes 79:Databases 2786:EC 5.3.1 2614:Kinetics 2538:Cofactor 2501:Activity 2122:glycerol 1949:Platelet 1819:Pyruvate 1593:NADH + H 1573:NADH + H 1457:aldolase 1215:11368170 845:17424909 765:See also 737:forms a 695:subunits 658:RCSB PDB 582:InterPro 505:arsenate 424:bacteria 252:) is an 230:proteins 218:articles 206:articles 163:RCSB PDB 2770:Biology 2724:Ligases 2494:Enzymes 2426:: other 2318:: C = C 2247:Ketoses 2243:Aldoses 2098:alanine 2074:lactate 2013:Enolase 1888:enzymes 1725:enolase 1319:Glucose 1266:PDBe-KB 1250:8130193 1180:2204418 1145:3311744 1104:9843453 1069:2005961 1029:2007138 994:2847777 959:6115415 918:2161683 799:PROSITE 594:PROSITE 562:PF00121 497:sulfate 466:enediol 454:diffuse 412:insects 408:mammals 381:5.3.1.1 379:Enzyme 354:  349:  316:  273:isomers 263:) that 261:5.3.1.1 185:QuickGO 150:profile 133:MetaCyc 68:CAS no. 61:5.3.1.1 2756:Portal 2698:Lyases 2424:5.3.99 2173:PFKFB4 2169:PFKFB3 2165:PFKFB2 2161:PFKFB1 1945:Muscle 1753:  1732:  1587:NAD+ P 1567:NAD+ P 1248:  1213:  1178:  1143:  1102:  1067:  1049:Nature 1027:  992:  957:  916:  883:999838 881:  843:  717:. The 673:PDBsum 647:  637:  619:SUPFAM 575:CL0036 548:Symbol 503:, and 422:, and 420:plants 392:C00118 370:C00111 278:and D- 269:triose 254:enzyme 213:PubMed 195:Search 181:AmiGO 169:PDBsum 109:ExPASy 97:BRENDA 85:IntEnz 56:EC no. 2650:Types 2413:PDIA3 2402:: S-S 2400:5.3.4 2316:5.3.3 2280:5.3.2 2239:5.3.1 2120:from 2096:from 2072:from 1941:Liver 691:dimer 615:SCOPe 606:SCOP2 416:fungi 145:PRIAM 2742:list 2735:EC7 2729:list 2722:EC6 2716:list 2709:EC5 2703:list 2696:EC4 2690:list 2683:EC3 2677:list 2670:EC2 2664:list 2657:EC1 2288:Enol 2284:Keto 2232:5.3) 2026:PKM2 2022:PKLR 1816:2 × 1768:2 × 1697:2 × 1657:2 × 1601:2 × 1537:2 × 1246:PMID 1211:PMID 1176:PMID 1141:PMID 1100:PMID 1065:PMID 1025:PMID 990:PMID 955:PMID 914:PMID 879:PMID 841:PMID 781:TPI1 666:PDBj 662:PDBe 645:ECOD 635:Pfam 611:1tph 571:clan 569:Pfam 557:Pfam 410:and 396:KEGG 385:KEGG 374:KEGG 225:NCBI 166:PDBe 121:KEGG 2349:EBP 2047:to 1951:)→/ 1924:)→/ 1918:HK3 1914:HK2 1910:HK1 1799:ATP 1796:ADP 1649:ATP 1646:ADP 1632:ATP 1629:ADP 1422:ADP 1419:ATP 1344:ADP 1341:ATP 1238:doi 1203:doi 1199:387 1168:doi 1131:doi 1127:168 1092:doi 1057:doi 1053:350 1017:doi 982:doi 945:doi 941:293 906:doi 871:doi 831:doi 797:in 653:PDB 551:TIM 394:at 383:at 372:at 250:TIM 248:or 246:TPI 201:PMC 157:PDB 2782:: 2282:: 2241:: 2230:EC 2171:, 2167:, 2163:, 2104:): 2080:): 2024:, 1977:, 1973:, 1947:, 1943:, 1920:, 1916:, 1912:, 1879:: 1875:: 1244:. 1234:33 1232:. 1209:. 1197:. 1174:. 1164:29 1162:. 1139:. 1125:. 1121:. 1098:. 1088:37 1086:. 1063:. 1051:. 1037:^ 1023:. 1013:30 1011:. 988:. 978:27 976:. 953:. 939:. 935:. 912:. 902:29 900:. 877:. 867:15 865:. 853:^ 839:. 827:58 825:. 821:. 664:; 660:; 643:/ 617:/ 613:/ 519:. 499:, 418:, 282:. 258:EC 183:/ 2758:: 2744:) 2740:( 2731:) 2727:( 2718:) 2714:( 2705:) 2701:( 2692:) 2688:( 2679:) 2675:( 2666:) 2662:( 2486:e 2479:t 2472:v 2435:/ 2415:) 2411:( 2351:) 2347:( 2286:/ 2245:/ 2228:( 2214:e 2207:t 2200:v 2124:: 2100:( 2076:( 2051:: 2028:) 2020:( 1981:) 1979:C 1975:B 1971:A 1955:← 1939:( 1928:← 1908:( 1883:/ 1865:e 1858:t 1851:v 1760:O 1758:2 1756:H 1739:O 1737:2 1735:H 1727:) 1723:( 1589:i 1569:i 1494:+ 1490:+ 1295:e 1288:t 1281:v 1252:. 1240:: 1217:. 1205:: 1182:. 1170:: 1147:. 1133:: 1106:. 1094:: 1071:. 1059:: 1031:. 1019:: 996:. 984:: 961:. 947:: 920:. 908:: 885:. 873:: 847:. 833:: 301:- 299:D 256:( 244:( 20:)

Index

Triosephosphateisomerase

EC no.
5.3.1.1
CAS no.
9023-78-3
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

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