686:
connected to the AOR enzyme primarily through pterin's
Hydrogen bonding networks with the amino acid residues. In addition, two water ligands that occupy the octahedral geometry take part in hydrogen bonding networks with pterin, phosphate, and Mg. While cluster is bound by four Cys ligands, Pterin - rich in amino and ether linkages - interacts with the Asp-X-X-Gly-Leu-(Cys/Asp) sequences in the AOR enzyme. In such sequence, Cys494 residue is also hydrogen bonded to the cluster. This indicates that Cys494 residue connects the Tungsten site and the cluster site in the enzyme. Iron atom in the cluster is additionally bound by three other Cystein ligands: . Also, another linker amino acid residue between ferredoxin cluster and pterin is the Arg76, which hydrogen bonds to both pterin and ferredoxin. It is proposed that such hydrogen bonding interactions imply pterin cyclic ring system as an electron carrier. Additionally the C=
1857:
671:
727:
630:, and isovalerdehyde, which is a metabolic product from common amino acids and glucose. For example, acetaldehyde reaches its kcat/KM value up to 22.0 ÎĽM-1s-1. In fact, some microorganisms only make use of amino acids as a carbon source, such as Thermococcus strain ES1; thus, they utilize aldehyde ferredoxin oxidoreductase to metabolize the amino acid carbon source.
209:
596:
substrates. Its primary role is to oxidize aldehyde coming derived from the metabolism of amino acids and glucoses. Aldehyde
Ferredoxin Oxidoreductase is a member of an AOR family, which includes glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR) and Formaldehyde Ferredoxin Oxidoreductase.
693:
AOR consists of three domains, domain 1, 2, and 3. While domain 1 contains pterin bound to tungsten, the other two domains provide a channel from tungsten to protein's surface (15 Angstroms in length) in order to allow specific substrates to enter the enzyme through its channel. In the active site,
749:
A tyrosine residue is proposed to activate the electrophilic centre of aldehydes by H-bonding to the carbonyl oxygen atom, coordinated to the W centre. A glutamic acid residue near the active site activates a water molecule for a nucleophilic attack on aldehyde carbonyl center. After nucleophilic
605:
AOR functions at high temperature conditions (~80 degrees
Celsius) at an optimal pH of 8-9. It is oxygen-sensitive as it loses bulk of its activity from oxygen exposure and works in the cytoplasm where it is a reducing environment. Thus, either exposure to oxygen or lowering of the temperature
750:
attack by water, hydride is transferred to oxo-tungsten sie thus, . Subsequently, W(VI) is regenerated by electron transfer to the 4Fe-4S center. With formaldehyde ferredoxin oxidoreductase, Glu308 and Tyr 416 would be involved while Glu313 and His448 is shown to be present in AOR active site.
685:
cofactors bind tungsten, as observed in many related enzymes. Tungsten is not bonded directly to the protein. Phosphate centers pendant on the cofactor are bound to a Mg, which is also bound by Asn93 and Ala183 to complete its octahedral coordination sphere. Thus, pterin and
Tungsten atoms are
702:
The iron center in between the two subunits serve a structural role in AOR. Iron metal atoms takes on a tetrahedral conformation while the ligand coordination comes from two histidines and glutamic acids. This is not known to have any functional role in the redox activity of the protein.
621:
incorporation. However, other proposals include its role in oxidation of amino acid metabolism aldehyde side products coming from de-aminated 2-ketoacids. The main substrates for aldehyde ferredoxin oxidoreductase are
1242:"The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway"
719:
In the catalytic cycle, W(VI) (tungsten "six") converts to W(IV) concomitant with oxidation of the aldehyde to a carboxylic acid (equivalently, a carboxylate). A W(V) intermediate can be detected by
694:
this pterin molecules is in a saddle-like conformation (500 to the normal plane) to “sit” on the domain 1 which also takes on a form with beta sheets to accommodate the
Tungsten-Pterin site.
1367:
1499:
437:
308:
163:
1423:
182:
999:"Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon
1398:
1360:
1044:"Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase"
606:
causes an irreversible loss of its catalytic properties. Also, as a result of oxygen sensitivity of AOR, purification of the enzyme is done under
569:
are not yet clear. AOR has been proposed to be the primary enzyme responsible for oxidising the aldehydes that are produced by the 2-keto acid
711:
cluster in AOR is different in some aspects to other ferredoxin molecules. EPR measurements confirm that it serves as a one-electron shuttle.
1896:
1353:
1327:
385:
256:
769:
Majumdar A, Sarkar S (May 2011). "Bioinorganic chemistry of molybdenum and tungsten enzymes: A structural–functional modeling approach".
1489:
1445:
1576:
1416:
1394:
1277:"Identification of molybdopterin as the organic component of the tungsten cofactor in four enzymes from hyperthermophilic Archaea"
175:
1519:
118:
1732:
648:
atoms. The two subunits are bridged by a low spin Iron center. It is believed that the two subunits function independently.
457:
328:
142:
958:"The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein"
1847:
917:"Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non-activated carboxylic acids to aldehydes"
639:
1411:
543:
1717:
1833:
1820:
1807:
1794:
1781:
1768:
1755:
1531:
1477:
1455:
1433:
1390:
1727:
577:
1681:
1624:
1381:
614:
511:, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The
478:
136:
29:
1535:
445:
316:
1629:
535:
123:
659:
in the active site of AOR adopts a distorted square pyramidal geometry bound an oxo/hydroxo ligand and the
1494:
1406:
1650:
1569:
187:
1722:
441:
312:
111:
46:
1055:
398:
269:
1686:
581:
41:
139:
1619:
627:
63:
1891:
1543:
1333:
1323:
1298:
1263:
1180:
1083:
1024:
979:
938:
897:
823:
690:
center of the pterin binds Na. The W=O center is proposed, not verified crystallographically.
493:
432:
303:
130:
1209:
Bevers LE, Hagedoorn PL, Hagen WR (February 2009). "The bioinorganic chemistry of tungsten".
1665:
1660:
1634:
1562:
1467:
1315:
1288:
1253:
1218:
1172:
1073:
1063:
1014:
969:
928:
887:
815:
778:
720:
424:
295:
1712:
1696:
1609:
570:
551:
512:
99:
1157:
800:
592:
ES-1 strain differ by their substrate specificity: AFOs show a broader size range of its
213:
structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
1345:
1059:
75:
1861:
1750:
1691:
1377:
1310:
Roy R, Menon AL, Adams MW (2001). "Aldehyde
Oxidoreductases from Pyrococcus furiosus".
974:
957:
933:
916:
892:
875:
508:
158:
34:
1319:
1293:
1276:
1258:
1241:
1885:
1655:
1614:
1176:
1078:
1043:
819:
682:
674:
664:
532:
390:
261:
561:, the sole member of the AOR family containing molybdenum. GAPOR may be involved in
531:
The active site of the AOR family feature an oxo-tungsten center bound to a pair of
366:
237:
1604:
623:
420:
291:
1877:
542:
cluster. This family includes AOR, formaldehyde ferredoxin oxidoreductase (FOR),
378:
249:
1828:
1763:
1599:
1856:
1514:
1437:
1222:
782:
660:
562:
470:
1802:
1776:
1481:
1068:
1019:
998:
554:
489:
1337:
726:
1302:
1267:
1184:
1087:
1028:
983:
942:
901:
827:
670:
394:
265:
208:
1873:
656:
593:
557:
found in clostridia; and hydroxycarboxylate viologen oxidoreductase from
373:
244:
607:
618:
566:
546:
ferredoxin oxidoreductase (GAPOR), all isolated from hyperthermophilic
481:
106:
87:
1815:
1585:
1509:
1504:
1459:
547:
539:
523:. It is a relatively rare example of a tungsten-containing protein.
485:
452:
323:
170:
82:
70:
58:
644:
AOR is homodimeric. Each 67kDa subunit contains 1 tungsten and 4-5
640:
Transition metal oxo complex § Molybdenum/tungsten oxo species
1789:
725:
669:
1158:"Molybdenum-cofactor-containing enzymes: structure and mechanism"
801:"Molybdenum-cofactor-containing enzymes: structure and mechanism"
1869:
645:
503:
O + 2 oxidized ferredoxin ⇌ an acid + 3 H + 2 reduced ferredoxin
414:
361:
285:
232:
94:
1558:
1349:
1128:
1126:
Roy R, Dhawan IK, Johnson MK, Rees DC, Adams MW (2006-04-15).
1554:
956:
Trautwein T, Krauss F, Lottspeich F, Simon H (June 1994).
746:
The redox equivalents are provided by the 4Fe-4S cluster.
617:(glucose degradation) due to its increased activity with
1275:
Johnson JL, Rajagopalan KV, Mukund S, Adams MW (1993).
915:
White H, Strobl G, Feicht R, Simon H (September 1989).
1868:
This article incorporates text from the public domain
1042:
Ma K, Hutchins A, Sung SJ, Adams MW (September 1997).
1845:
1500:
Branched-chain alpha-keto acid dehydrogenase complex
1741:
1705:
1674:
1643:
1592:
1530:
1476:
1454:
1432:
1389:
1314:. Methods Enzymol. Vol. 331. pp. 132–44.
451:
431:
413:
408:
384:
372:
360:
352:
347:
342:
322:
302:
284:
279:
255:
243:
231:
223:
218:
201:
181:
169:
157:
152:
129:
117:
105:
93:
81:
69:
57:
52:
40:
28:
23:
18:
677:cofactor, shown in the dithiol protonation state.
1424:Mycothiol-dependent formaldehyde dehydrogenase
869:
867:
865:
863:
861:
859:
857:
1570:
1361:
855:
853:
851:
849:
847:
845:
843:
841:
839:
837:
794:
792:
8:
715:Aldehyde ferredoxin oxidoreductase mechanism
538:(which does not contain molybdenum) and an
1577:
1563:
1555:
1368:
1354:
1346:
613:It is proposed that AOR has a role in the
405:
276:
207:
149:
1292:
1257:
1130:(5 ed.). John Wiley & Sons, Ltd.
1077:
1067:
1018:
973:
932:
891:
1204:
1202:
1200:
1198:
1196:
1194:
1156:Kisker C, Schindelin H, Rees DC (1997).
799:Kisker C, Schindelin H, Rees DC (1997).
1852:
1121:
1119:
1117:
764:
762:
758:
1151:
1149:
1147:
1145:
1143:
1141:
1139:
1137:
1115:
1113:
1111:
1109:
1107:
1105:
1103:
1101:
1099:
1097:
339:
198:
15:
507:This enzyme belongs to the family of
7:
734:General Reaction Mechanism of AOR:
1490:Oxoglutarate dehydrogenase complex
1446:Formate dehydrogenase (cytochrome)
975:10.1111/j.1432-1033.1994.tb18954.x
934:10.1111/j.1432-1033.1989.tb14993.x
893:10.1111/j.1574-6976.1996.tb00226.x
874:Kletzin A, Adams MW (March 1996).
517:aldehyde:ferredoxin oxidoreductase
475:aldehyde ferredoxin oxidoreductase
19:Aldehyde ferredoxin oxidoreductase
14:
1417:Long-chain-aldehyde dehydrogenase
997:Mukund S, Adams MW (April 1995).
730:AOR mechanism at the active site.
565:, but the functions of the other
1855:
1312:Hyperthermophilic enzymes Part B
1177:10.1146/annurev.biochem.66.1.233
876:"Tungsten in biological systems"
820:10.1146/annurev.biochem.66.1.233
1211:Coordination Chemistry Reviews
771:Coordination Chemistry Reviews
1:
1320:10.1016/S0076-6879(01)31052-2
1294:10.1016/S0021-9258(18)53474-8
1259:10.1016/S0021-9258(18)98669-2
1165:Annual Review of Biochemistry
519:. This enzyme is also called
409:Available protein structures:
280:Available protein structures:
1897:Enzymes of unknown structure
1048:Proc. Natl. Acad. Sci. U.S.A
1240:Mukund S, Adams MW (1991).
1913:
1867:
1412:Acetaldehyde dehydrogenase
637:
578:hyperthermophillic archaea
544:glyceraldehyde-3-phosphate
1733:Michaelis–Menten kinetics
1223:10.1016/j.ccr.2008.01.017
783:10.1016/j.ccr.2010.11.027
404:
275:
206:
148:
1625:Diffusion-limited enzyme
615:Entner-Doudoroff pathway
515:of this enzyme class is
1069:10.1073/pnas.94.18.9608
1020:10.1074/jbc.270.15.8389
1495:Pyruvate dehydrogenase
1407:Aldehyde dehydrogenase
731:
678:
1718:Eadie–Hofstee diagram
1651:Allosteric regulation
729:
673:
1728:Lineweaver–Burk plot
663:substituents of two
1536:iron–sulfur protein
1060:1997PNAS...94.9608M
1001:Pyrococcus furiosus
880:FEMS Microbiol. Rev
777:(9–10): 1039–1054.
738:RCHO + H2O → RCO
582:Pyrococcus furiosus
1687:Enzyme superfamily
1620:Enzyme promiscuity
808:Annu. Rev. Biochem
732:
679:
628:phenylacetaldehyde
1843:
1842:
1552:
1551:
1544:Pyruvate synthase
1329:978-0-12-182232-3
494:chemical reaction
467:
466:
463:
462:
458:structure summary
338:
337:
334:
333:
329:structure summary
197:
196:
193:
192:
112:metabolic pathway
1904:
1860:
1859:
1851:
1723:Hanes–Woolf plot
1666:Enzyme activator
1661:Enzyme inhibitor
1635:Enzyme catalysis
1579:
1572:
1565:
1556:
1468:Aldehyde oxidase
1370:
1363:
1356:
1347:
1341:
1306:
1296:
1271:
1261:
1252:(22): 14208–16.
1227:
1226:
1217:(3–4): 269–290.
1206:
1189:
1188:
1162:
1153:
1132:
1131:
1123:
1092:
1091:
1081:
1071:
1039:
1033:
1032:
1022:
994:
988:
987:
977:
953:
947:
946:
936:
912:
906:
905:
895:
871:
832:
831:
805:
796:
787:
786:
766:
721:EPR spectroscopy
588:ES-4 strain and
584:. The archaeons
576:AOR is found in
559:Proteus vulgaris
406:
340:
277:
211:
199:
150:
16:
1912:
1911:
1907:
1906:
1905:
1903:
1902:
1901:
1882:
1881:
1880:
1866:
1854:
1846:
1844:
1839:
1751:Oxidoreductases
1737:
1713:Enzyme kinetics
1701:
1697:List of enzymes
1670:
1639:
1610:Catalytic triad
1588:
1583:
1553:
1548:
1526:
1472:
1450:
1428:
1385:
1378:oxidoreductases
1374:
1344:
1330:
1309:
1274:
1239:
1235:
1233:Further reading
1230:
1208:
1207:
1192:
1160:
1155:
1154:
1135:
1125:
1124:
1095:
1054:(18): 9608–13.
1041:
1040:
1036:
1013:(15): 8389–92.
996:
995:
991:
962:Eur. J. Biochem
955:
954:
950:
921:Eur. J. Biochem
914:
913:
909:
873:
872:
835:
803:
798:
797:
790:
768:
767:
760:
756:
742:H + 2H + 2 e
741:
717:
652:Tungsten-pterin
642:
636:
603:
571:oxidoreductases
552:carboxylic acid
529:
513:systematic name
509:oxidoreductases
502:
499:an aldehyde + H
214:
12:
11:
5:
1910:
1908:
1900:
1899:
1894:
1884:
1883:
1865:
1864:
1841:
1840:
1838:
1837:
1824:
1811:
1798:
1785:
1772:
1759:
1745:
1743:
1739:
1738:
1736:
1735:
1730:
1725:
1720:
1715:
1709:
1707:
1703:
1702:
1700:
1699:
1694:
1689:
1684:
1678:
1676:
1675:Classification
1672:
1671:
1669:
1668:
1663:
1658:
1653:
1647:
1645:
1641:
1640:
1638:
1637:
1632:
1627:
1622:
1617:
1612:
1607:
1602:
1596:
1594:
1590:
1589:
1584:
1582:
1581:
1574:
1567:
1559:
1550:
1549:
1547:
1546:
1540:
1538:
1528:
1527:
1525:
1524:
1523:
1522:
1517:
1512:
1507:
1497:
1492:
1486:
1484:
1474:
1473:
1471:
1470:
1464:
1462:
1452:
1451:
1449:
1448:
1442:
1440:
1430:
1429:
1427:
1426:
1421:
1420:
1419:
1414:
1403:
1401:
1387:
1386:
1375:
1373:
1372:
1365:
1358:
1350:
1343:
1342:
1328:
1307:
1287:(7): 4848–52.
1272:
1236:
1234:
1231:
1229:
1228:
1190:
1133:
1093:
1034:
989:
968:(3): 1025–32.
948:
907:
833:
788:
757:
755:
752:
744:
743:
739:
716:
713:
709:
708:
700:
699:
654:
653:
635:
632:
610:environments.
602:
599:
528:
525:
505:
504:
500:
465:
464:
461:
460:
455:
449:
448:
435:
429:
428:
418:
411:
410:
402:
401:
388:
382:
381:
376:
370:
369:
364:
358:
357:
354:
350:
349:
345:
344:
336:
335:
332:
331:
326:
320:
319:
306:
300:
299:
289:
282:
281:
273:
272:
259:
253:
252:
247:
241:
240:
235:
229:
228:
225:
221:
220:
216:
215:
212:
204:
203:
195:
194:
191:
190:
185:
179:
178:
173:
167:
166:
161:
155:
154:
146:
145:
134:
127:
126:
121:
115:
114:
109:
103:
102:
97:
91:
90:
85:
79:
78:
73:
67:
66:
61:
55:
54:
50:
49:
44:
38:
37:
32:
26:
25:
21:
20:
13:
10:
9:
6:
4:
3:
2:
1909:
1898:
1895:
1893:
1890:
1889:
1887:
1879:
1875:
1871:
1863:
1858:
1853:
1849:
1835:
1831:
1830:
1825:
1822:
1818:
1817:
1812:
1809:
1805:
1804:
1799:
1796:
1792:
1791:
1786:
1783:
1779:
1778:
1773:
1770:
1766:
1765:
1760:
1757:
1753:
1752:
1747:
1746:
1744:
1740:
1734:
1731:
1729:
1726:
1724:
1721:
1719:
1716:
1714:
1711:
1710:
1708:
1704:
1698:
1695:
1693:
1692:Enzyme family
1690:
1688:
1685:
1683:
1680:
1679:
1677:
1673:
1667:
1664:
1662:
1659:
1657:
1656:Cooperativity
1654:
1652:
1649:
1648:
1646:
1642:
1636:
1633:
1631:
1628:
1626:
1623:
1621:
1618:
1616:
1615:Oxyanion hole
1613:
1611:
1608:
1606:
1603:
1601:
1598:
1597:
1595:
1591:
1587:
1580:
1575:
1573:
1568:
1566:
1561:
1560:
1557:
1545:
1542:
1541:
1539:
1537:
1533:
1529:
1521:
1518:
1516:
1513:
1511:
1508:
1506:
1503:
1502:
1501:
1498:
1496:
1493:
1491:
1488:
1487:
1485:
1483:
1479:
1475:
1469:
1466:
1465:
1463:
1461:
1457:
1453:
1447:
1444:
1443:
1441:
1439:
1435:
1431:
1425:
1422:
1418:
1415:
1413:
1410:
1409:
1408:
1405:
1404:
1402:
1400:
1396:
1392:
1388:
1383:
1379:
1376:Aldehyde/oxo
1371:
1366:
1364:
1359:
1357:
1352:
1351:
1348:
1339:
1335:
1331:
1325:
1321:
1317:
1313:
1308:
1304:
1300:
1295:
1290:
1286:
1282:
1281:J. Biol. Chem
1278:
1273:
1269:
1265:
1260:
1255:
1251:
1247:
1246:J. Biol. Chem
1243:
1238:
1237:
1232:
1224:
1220:
1216:
1212:
1205:
1203:
1201:
1199:
1197:
1195:
1191:
1186:
1182:
1178:
1174:
1170:
1166:
1159:
1152:
1150:
1148:
1146:
1144:
1142:
1140:
1138:
1134:
1129:
1122:
1120:
1118:
1116:
1114:
1112:
1110:
1108:
1106:
1104:
1102:
1100:
1098:
1094:
1089:
1085:
1080:
1075:
1070:
1065:
1061:
1057:
1053:
1049:
1045:
1038:
1035:
1030:
1026:
1021:
1016:
1012:
1008:
1007:J. Biol. Chem
1004:
1002:
993:
990:
985:
981:
976:
971:
967:
963:
959:
952:
949:
944:
940:
935:
930:
926:
922:
918:
911:
908:
903:
899:
894:
889:
885:
881:
877:
870:
868:
866:
864:
862:
860:
858:
856:
854:
852:
850:
848:
846:
844:
842:
840:
838:
834:
829:
825:
821:
817:
813:
809:
802:
795:
793:
789:
784:
780:
776:
772:
765:
763:
759:
753:
751:
747:
737:
736:
735:
728:
724:
722:
714:
712:
706:
705:
704:
697:
696:
695:
691:
689:
684:
683:molybdopterin
676:
675:Molybdopterin
672:
668:
666:
665:molybdopterin
662:
658:
651:
650:
649:
647:
641:
633:
631:
629:
625:
620:
616:
611:
609:
600:
598:
595:
591:
587:
583:
579:
574:
572:
568:
564:
560:
556:
553:
549:
545:
541:
537:
534:
533:molybdopterin
526:
524:
522:
518:
514:
510:
498:
497:
496:
495:
491:
487:
483:
480:
476:
472:
459:
456:
454:
450:
447:
443:
439:
436:
434:
430:
426:
422:
419:
416:
412:
407:
403:
400:
396:
392:
389:
387:
383:
380:
377:
375:
371:
368:
365:
363:
359:
355:
351:
346:
341:
330:
327:
325:
321:
318:
314:
310:
307:
305:
301:
297:
293:
290:
287:
283:
278:
274:
271:
267:
263:
260:
258:
254:
251:
248:
246:
242:
239:
236:
234:
230:
226:
222:
217:
210:
205:
200:
189:
186:
184:
180:
177:
174:
172:
168:
165:
162:
160:
156:
151:
147:
144:
141:
138:
135:
132:
128:
125:
122:
120:
116:
113:
110:
108:
104:
101:
98:
96:
92:
89:
88:NiceZyme view
86:
84:
80:
77:
74:
72:
68:
65:
62:
60:
56:
51:
48:
45:
43:
39:
36:
33:
31:
27:
22:
17:
1829:Translocases
1826:
1813:
1800:
1787:
1774:
1764:Transferases
1761:
1748:
1605:Binding site
1311:
1284:
1280:
1249:
1245:
1214:
1210:
1168:
1164:
1127:
1051:
1047:
1037:
1010:
1006:
1000:
992:
965:
961:
951:
927:(1): 89–96.
924:
920:
910:
883:
879:
811:
807:
774:
770:
748:
745:
733:
718:
710:
707:Fe4S4 centre
701:
692:
687:
680:
655:
643:
624:acetaldehyde
612:
604:
590:Thermococcus
589:
585:
575:
558:
530:
520:
516:
506:
474:
468:
76:BRENDA entry
47:138066-90-7
1600:Active site
886:(1): 5–63.
667:cofactors.
348:Identifiers
219:Identifiers
64:IntEnz view
24:Identifiers
1886:Categories
1803:Isomerases
1777:Hydrolases
1644:Regulation
1438:cytochrome
1171:: 233–67.
814:: 233–67.
754:References
661:dithiolene
638:See also:
586:Pyrococcus
563:glycolysis
527:Occurrence
471:enzymology
421:structures
292:structures
133:structures
100:KEGG entry
1878:IPR013983
1682:EC number
1482:disulfide
634:Structure
555:reductase
536:cofactors
490:catalyzes
379:IPR001203
250:IPR013983
53:Databases
1892:EC 1.2.7
1874:InterPro
1706:Kinetics
1630:Cofactor
1593:Activity
1338:11265456
657:Tungsten
601:Function
594:aldehyde
567:proteins
484:) is an
438:RCSB PDB
374:InterPro
309:RCSB PDB
245:InterPro
188:proteins
176:articles
164:articles
137:RCSB PDB
1862:Biology
1816:Ligases
1586:Enzymes
1303:8444863
1268:1907273
1185:9242907
1088:9275170
1056:Bibcode
1029:7721730
984:8026480
943:2550230
902:8672295
828:9242907
619:maltose
482:1.2.7.5
367:PF01314
238:PF02730
124:profile
107:MetaCyc
42:CAS no.
35:1.2.7.5
1848:Portal
1790:Lyases
1510:BCKDHB
1505:BCKDHA
1460:oxygen
1336:
1326:
1301:
1266:
1183:
1086:
1076:
1027:
982:
941:
900:
826:
608:anoxic
548:archea
540:4Fe-4S
486:enzyme
453:PDBsum
427:
417:
399:SUPFAM
356:AFOR_C
353:Symbol
343:AFOR_C
324:PDBsum
298:
288:
270:SUPFAM
227:AFOR_N
224:Symbol
202:AFOR_N
171:PubMed
153:Search
143:PDBsum
83:ExPASy
71:BRENDA
59:IntEnz
30:EC no.
1742:Types
1532:1.2.7
1478:1.2.4
1456:1.2.3
1434:1.2.2
1391:1.2.1
1161:(PDF)
1079:23233
804:(PDF)
488:that
473:, an
395:SCOPe
386:SCOP2
266:SCOPe
257:SCOP2
119:PRIAM
1872:and
1870:Pfam
1834:list
1827:EC7
1821:list
1814:EC6
1808:list
1801:EC5
1795:list
1788:EC4
1782:list
1775:EC3
1769:list
1762:EC2
1756:list
1749:EC1
1399:NADP
1384:1.2)
1334:PMID
1324:ISBN
1299:PMID
1264:PMID
1181:PMID
1084:PMID
1025:PMID
980:PMID
939:PMID
898:PMID
824:PMID
698:Iron
681:Two
646:Iron
492:the
446:PDBj
442:PDBe
425:ECOD
415:Pfam
391:1aor
362:Pfam
317:PDBj
313:PDBe
296:ECOD
286:Pfam
262:1aor
233:Pfam
183:NCBI
140:PDBe
95:KEGG
1520:DLD
1515:DBT
1397:or
1395:NAD
1316:doi
1289:doi
1285:268
1254:doi
1250:266
1219:doi
1215:253
1173:doi
1074:PMC
1064:doi
1015:doi
1011:270
970:doi
966:222
929:doi
925:184
888:doi
816:doi
779:doi
775:255
521:AOR
469:In
433:PDB
304:PDB
159:PMC
131:PDB
1888::
1876::
1534::
1480::
1458::
1436::
1393::
1382:EC
1332:.
1322:.
1297:.
1283:.
1279:.
1262:.
1248:.
1244:.
1213:.
1193:^
1179:.
1169:66
1167:.
1163:.
1136:^
1096:^
1082:.
1072:.
1062:.
1052:94
1050:.
1046:.
1023:.
1009:.
1005:.
978:.
964:.
960:.
937:.
923:.
919:.
896:.
884:18
882:.
878:.
836:^
822:.
812:66
810:.
806:.
791:^
773:.
761:^
723:.
626:,
580:,
573:.
550:;
479:EC
444:;
440:;
423:/
397:/
393:/
315:;
311:;
294:/
268:/
264:/
1850::
1836:)
1832:(
1823:)
1819:(
1810:)
1806:(
1797:)
1793:(
1784:)
1780:(
1771:)
1767:(
1758:)
1754:(
1578:e
1571:t
1564:v
1380:(
1369:e
1362:t
1355:v
1340:.
1318::
1305:.
1291::
1270:.
1256::
1225:.
1221::
1187:.
1175::
1090:.
1066::
1058::
1031:.
1017::
1003:"
986:.
972::
945:.
931::
904:.
890::
830:.
818::
785:.
781::
740:2
688:O
501:2
477:(
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