401:
489:
389:
477:
413:
1875:
464:
from binding the enzyme, making FRP an FMN specific flavin reductase. The placement of methyl groups in the isoalloxazine ring can also have an effect on the binding and specificity of the enzyme for substrate. There is a depletion of a C-terminal extension that allows for the binding of NADPH, and
427:
made up of two subunits. Each subunit is similar. Flavin reductase P, FRP, was studied by Tanner, Lei, Tu and Krause and was discovered to have a structure made up of two subunits each containing a sandwich domain and an excursion domain. The excursion domains of each subunit reach out to connect the
218:
a class of enzymes. There are a variety of flavin reductases, (i.e. FRP, FRE, FRG, etc.) which bind free flavins and through hydrogen bonding, catalyze the reduction of these molecules to a reduced flavin. Riboflavin, or vitamin B, and flavin mononucleotide are two of the most well known
647:
which has been shown to increase the effectiveness of the prodrugs for cancerous tumors. A dual flavin reductase has been shown to participate in the activation of anticancer drugs. There are also molecules that when oxidized can be
614:
assists the body in maintaining homeostatic microbiota. A study showed that women with lactobacillus that produced hydrogen peroxide were less likely to develop bacterial vaginosis prebirth. It was also seen in
488:
503:
of the flavin reductase process is described above and most likely follows the ping pong kinetic pattern. This means that it is a bisubstrate-biproduct mechanism. First the flavin reductase enzyme binds
1080:
Tinikul R, Pisawong W, Sucharitakul J, Nijvipakul S, Ballou DP, Chaiyen P (1 Oct 2013). "The transfer of reduced flavin mononucleotide from LuxG oxidoreductase to luciferase via free diffusion".
572:
concentration of flavin reductase was increased. This suggests a connection between either a flavin reductase-luciferase complex or reduced flavin and the luminescence process in
277:
989:
771:
Yubisui T, Takeshita M, Yoneyama Y (June 1980). "Reduction of methemoglobin through flavin at the physiological concentration by NADPH-flavin reductase of human erythrocytes".
1540:
528:. Then, reduced flavin is released from flavin reductase as the second product. In this way, the reduction of flavin is dependent on flavin reductase binding first to
476:
179:
1435:
1288:"The Flavin Reductase MsuE is a Novel Nitroreductase that can efficiently Activate two promising next Generation Prodrugs for Gene-Directed Enzyme Prodrug Therapy"
400:
198:
1465:
299:
287:
227:
in erythrocytes. Flavin reductases are similar and often confused for ferric reductases because of their similar catalytic mechanism and structures.
388:
1905:
1484:
1428:
1507:
1594:
1461:
896:
Takahito
Imagawa; Toshiharu Tsurumura; Yasasushi Sugimoto; Kenji Aki; Kazumi Ishido; Seiki Kuramitsu; Hideaki Tsuge (3 Nov 2011).
1900:
191:
576:. The bacteria oxidize the reduced flavin mononucleotide to oxidized FMN and transfer it through free fusion to generate light.
623:
because flavin reductase has an antioxidative effect, which decreases oxygen levels, maintaining the metronidazole population.
1421:
1379:
856:
Tanner, JJ; B. Lei; SC Tu; KL Krause (22 Oct 1996). "Flavin
Reductase P: Structure of a Dimeric Enzyme That Reduces Flavin".
142:
118:
1750:
1174:
Production in species of the lactobacillus acidophilus group, a central role for a novel NADPH dependent flavin reductase"
1865:
1382:, Xun L (31 May 2002). "A bacterial flavin reductase system reduces chromate to a soluble chromium(III)-NAD(+) complex".
494:
The ping pong mechanism is shown with NADPH binding first and leaving as NADP+ before FMN is bound by Flavin
Reductase.
412:
461:
722:"Functional Assembly of camphor converting two-component Baeyer–Villiger monooxygenases with a flavin reductase from
223:
in the body and are used in a variety of processes which include metabolism of fat and ketones and the reduction of
1479:
1735:
1164:
Hertzberger R; Arents Jos; Dekker H; Pridmore R; Gysler C; Kleerebezem M; Teixeira de Mattos M (31 January 2014).
652:. In this case, it is helpful to have flavin reductase to reduce these molecules, such as carcinogenic chromate.
1851:
1838:
1825:
1812:
1799:
1786:
1773:
1527:
1494:
1457:
1745:
136:
1699:
1642:
1448:
291:
239:
29:
123:
1647:
1561:
1556:
1474:
806:
Marc
Fontecave; Jacques Coves; Jean-Louis Pierre (27 April 1993). "Ferric reductases or flavin reductases".
643:. However, current research is showing an interest in these reductase molecules, specifically, MSuE from
449:
262:
203:
1668:
1587:
616:
445:
111:
1740:
46:
1185:
1337:
Paine MJ, Garner AP, Powell D, Sibbald J, Sales M, Pratt N, Smith T, Tew DG, Wolf CR (14 Jan 2000).
1229:
Leitsch, David; Janssen, Brian D.; Kolarich, Daniel; Johnson, Patricia J.; DuchĂŞne, Michael (2014).
990:"Role of the C-terminal extension stacked on the re-face of the isoalloxazine ring moiety of flavin"
520:
is released and then the flavin substrate is bound to the enzyme. In this step, the hydride attacks
1704:
283:
139:
41:
1037:
Warren Duane; JW Hastings (10 June 1974). "Flavin
Nomonucleotide Reductase of Luminous Bacteria".
949:"The Mechanism and Substrate specificity of the NADPH:Flavin Oxidoreductase from Escherichia Coli"
898:"Structural Basis of Free Reduced Flavin Generation by Flavin Reductase from Thermus Thermophilus"
63:
1637:
1062:
831:
753:
500:
1895:
1512:
1399:
1360:
1319:
1286:
Green LK, Storey MA, Williams EM, Patterson AV, Smaill JB, Copp JN, Ackerley DF (8 Aug 2013).
1268:
1250:
1211:
1146:
1097:
1054:
1019:
970:
929:
873:
823:
788:
745:
702:
603:
254:
130:
460:
side chains of flavin reductase. Side chains 167–169 in FRP block the isoalloxazine ring in
1683:
1678:
1652:
1580:
1391:
1350:
1309:
1299:
1258:
1242:
1201:
1193:
1136:
1128:
1089:
1046:
1009:
1001:
960:
919:
909:
865:
815:
780:
737:
692:
682:
313:, specifically those acting on the CH-NH group of donors with NAD or NADP as acceptor. The
99:
1730:
1714:
1627:
1517:
784:
565:
549:
314:
721:
75:
1189:
516:, it is not possible for the enzyme to bind both NADPH and the flavin. For this reason,
34:
1879:
1768:
1709:
1444:
1314:
1287:
1263:
1230:
1206:
1165:
1141:
1116:
924:
897:
697:
670:
453:
310:
174:
1395:
154:
1889:
1673:
1632:
640:
620:
588:
437:
424:
224:
149:
1066:
835:
757:
1622:
649:
602:
It has also been suggested that flavin reductases play a role in the production of
303:
220:
1413:
1231:"Trichomonas vaginalisflavin reductase 1 and its role in metronidazole resistance"
465:
studies show that if it is removed, it is depleted, catalytic activity increases.
1005:
1846:
1781:
1617:
592:
525:
429:
158:
1874:
1117:"Evidence that biliverdin-IX beta reductase and flavin reductase are identical"
631:
Currently, it is seen that bacterial flavin reductase can be used to sensitize
482:
This shows the hydrogen bonding of flavin reductase with flavin mononucleotide.
741:
553:
457:
295:
231:
1254:
965:
948:
687:
1820:
1794:
914:
632:
250:
1403:
1364:
1355:
1338:
1323:
1304:
1272:
1215:
1101:
1023:
933:
749:
706:
1150:
974:
877:
827:
792:
1197:
580:
573:
545:
521:
1058:
720:
Kadow M, Balke K, Willetts A, Bornscheuer UT, Bäckvall JE (5 Nov 2013).
242:
87:
1531:
1050:
819:
509:
106:
1246:
1132:
1093:
1014:
869:
1833:
1603:
1498:
1339:"Cloning and Characterization of a novel human dual flavin reductase"
947:
Fieschi F, Niviere V, Frier C, Decout JL, Fontecave M (22 Dec 1995).
517:
513:
448:
substrate. The isoalloxazine ring of flavin mononucleotide is where
433:
246:
186:
82:
70:
58:
639:
to pro drugs. At first, flavin reductases were used to target the
327:
riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide
619:
that decreased levels of flavin reductase increased the cycling of
1807:
636:
596:
584:
529:
505:
441:
533:
94:
1576:
1417:
452:
occurs. Therefore, this is where flavin creates a variety of
587:
dependent reduction of flavin mononucleotide which occurs in
428:
sandwich domain of the other subunit. This creates a large
1572:
671:"Flavoprotein monooxegenases for oxidative biocatalysis"
266:
1115:
Shalloe F, Elliott G, Ennis O, Mantle TJ (1 Jun 1996).
406:
This is the structure of reduced flavin mononucleotide.
1863:
265:
1759:
1723:
1692:
1661:
1610:
1549:
1526:
1493:
1456:
988:Seo D, Asano T, Komori H, Sakurai T (30 Jan 2014).
197:
185:
173:
168:
148:
129:
117:
105:
93:
81:
69:
57:
52:
40:
28:
23:
18:
271:
1541:Electron-transferring-flavoprotein dehydrogenase
552:organisms, flavin reductase is important in the
394:This is the structure of flavin mononucleotide.
669:Ceccoli RD, Bianchi DA, Rial DV (6 Feb 2014).
1588:
1429:
8:
1595:
1581:
1573:
1436:
1422:
1414:
606:. This would be biologically helpful as H
286:of this enzyme are reduced riboflavin and
165:
1354:
1313:
1303:
1262:
1205:
1140:
1013:
964:
923:
913:
696:
686:
264:
851:
849:
847:
845:
544:Flavin reductases exist in a variety of
524:on the flavin, which allows for another
1870:
661:
472:
384:
319:reduced-riboflavin:NADP+ oxidoreductase
15:
891:
889:
887:
785:10.1093/oxfordjournals.jbchem.a132915
548:, including animals and bacteria. In
309:This enzyme belongs to the family of
7:
381:Structures of reactants and products
367:riboflavine mononucleotide reductase
321:. Other names in common use include
1485:Methylenetetrahydrofolate reductase
1378:Puzon GJ, Petersen JN, Roberts AG,
363:riboflavin mononucleotide reductase
272:{\displaystyle \rightleftharpoons }
1508:Dihydrobenzophenanthridine oxidase
579:In humans, flavin reductase often
508:and stabilizes the release of the
14:
556:process. In an experiment with
1873:
487:
475:
411:
399:
387:
375:NADPH2:riboflavin oxidoreductase
339:flavine mononucleotide reductase
335:flavin mononucleotide reductase
432:core in flavin reductase The
418:This is the structure of NADP+
279:reduced riboflavin + NADP + H
1:
1396:10.1016/S0006-291X(02)00438-2
1384:Biochem. Biophys. Res. Commun
371:NADPH2 dehydrogenase (flavin)
347:NADPH-dependent FMN reductase
1906:Enzymes of unknown structure
1006:10.1016/j.plaphy.2014.01.011
359:NADPH-specific FMN reductase
730:Appl. Microbiol. Biotechnol
323:NADPH:flavin oxidoreductase
1922:
1480:Saccharopine dehydrogenase
1751:Michaelis–Menten kinetics
742:10.1007/s00253-013-5338-3
164:
1643:Diffusion-limited enzyme
1178:Appl. Environ. Microbiol
966:10.1074/jbc.270.51.30392
688:10.3389/fmicb.2014.00025
317:of this enzyme class is
1901:NADPH-dependent enzymes
1562:Cytokinin dehydrogenase
1557:Sarcosine dehydrogenase
1475:Dihydrofolate reductase
915:10.1074/jbc.M111.257824
259:riboflavin + NADPH + H
1356:10.1074/jbc.275.2.1471
1305:10.3390/cancers5030985
1235:Molecular Microbiology
994:Plant Physiol. Biochem
645:Pseudomonas aeruginosa
423:Flavin reductase is a
351:NADPH-flavin reductase
273:
1736:Eadie–Hofstee diagram
1669:Allosteric regulation
617:Trichomonas vaginalis
568:was increased as the
446:flavin mononucleotide
343:FMN reductase (NADPH)
274:
1746:Lineweaver–Burk plot
1198:10.1128/AEM.04272-13
627:Future of the enzyme
331:phosphate) reductase
263:
1190:2014ApEnM..80.2229H
540:Biological function
532:, or in some cases
355:NADPH-FMN reductase
1705:Enzyme superfamily
1638:Enzyme promiscuity
1051:10.1007/BF01731866
1039:Mol. Cell. Biochem
820:10.1007/bf00205187
456:to connect to the
269:
1861:
1860:
1570:
1569:
1513:Sarcosine oxidase
1247:10.1111/mmi.12455
1133:10.1042/bj3160385
1094:10.1021/bi4006545
959:(51): 30392–400.
870:10.1021/bi961400v
641:hypoxia of tumors
604:hydrogen peroxide
255:chemical reaction
213:
212:
209:
208:
112:metabolic pathway
1913:
1878:
1877:
1869:
1741:Hanes–Woolf plot
1684:Enzyme activator
1679:Enzyme inhibitor
1653:Enzyme catalysis
1597:
1590:
1583:
1574:
1438:
1431:
1424:
1415:
1408:
1407:
1375:
1369:
1368:
1358:
1334:
1328:
1327:
1317:
1307:
1283:
1277:
1276:
1266:
1226:
1220:
1219:
1209:
1161:
1155:
1154:
1144:
1112:
1106:
1105:
1077:
1071:
1070:
1034:
1028:
1027:
1017:
985:
979:
978:
968:
944:
938:
937:
927:
917:
908:(51): 44078–85.
893:
882:
881:
853:
840:
839:
803:
797:
796:
768:
762:
761:
717:
711:
710:
700:
690:
666:
491:
479:
444:and one for the
415:
403:
391:
290:, whereas its 3
278:
276:
275:
270:
236:flavin reductase
216:Flavin reductase
166:
19:flavin reductase
16:
1921:
1920:
1916:
1915:
1914:
1912:
1911:
1910:
1886:
1885:
1884:
1872:
1864:
1862:
1857:
1769:Oxidoreductases
1755:
1731:Enzyme kinetics
1719:
1715:List of enzymes
1688:
1657:
1628:Catalytic triad
1606:
1601:
1571:
1566:
1545:
1522:
1518:Proline oxidase
1489:
1452:
1445:Oxidoreductases
1442:
1412:
1411:
1377:
1376:
1372:
1336:
1335:
1331:
1292:Cancers (Basel)
1285:
1284:
1280:
1228:
1227:
1223:
1173:
1169:
1163:
1162:
1158:
1114:
1113:
1109:
1088:(39): 6834–43.
1079:
1078:
1074:
1036:
1035:
1031:
987:
986:
982:
946:
945:
941:
895:
894:
885:
864:(42): 13531–9.
855:
854:
843:
805:
804:
800:
770:
769:
765:
719:
718:
714:
675:Front Microbiol
668:
667:
663:
658:
629:
613:
609:
566:bioluminescence
542:
495:
492:
483:
480:
471:
419:
416:
407:
404:
395:
392:
383:
315:systematic name
311:oxidoreductases
261:
260:
12:
11:
5:
1919:
1917:
1909:
1908:
1903:
1898:
1888:
1887:
1883:
1882:
1859:
1858:
1856:
1855:
1842:
1829:
1816:
1803:
1790:
1777:
1763:
1761:
1757:
1756:
1754:
1753:
1748:
1743:
1738:
1733:
1727:
1725:
1721:
1720:
1718:
1717:
1712:
1707:
1702:
1696:
1694:
1693:Classification
1690:
1689:
1687:
1686:
1681:
1676:
1671:
1665:
1663:
1659:
1658:
1656:
1655:
1650:
1645:
1640:
1635:
1630:
1625:
1620:
1614:
1612:
1608:
1607:
1602:
1600:
1599:
1592:
1585:
1577:
1568:
1567:
1565:
1564:
1559:
1553:
1551:
1547:
1546:
1544:
1543:
1537:
1535:
1524:
1523:
1521:
1520:
1515:
1510:
1504:
1502:
1491:
1490:
1488:
1487:
1482:
1477:
1471:
1469:
1454:
1453:
1443:
1441:
1440:
1433:
1426:
1418:
1410:
1409:
1370:
1329:
1278:
1241:(1): 198–208.
1221:
1184:(7): 2229–39.
1171:
1167:
1156:
1107:
1072:
1029:
980:
939:
883:
841:
798:
779:(6): 1715–20.
763:
736:(9): 3975–86.
712:
660:
659:
657:
654:
628:
625:
611:
607:
541:
538:
512:. Because of
497:
496:
493:
486:
484:
481:
474:
470:
467:
454:hydrogen bonds
421:
420:
417:
410:
408:
405:
398:
396:
393:
386:
382:
379:
282:Thus, the two
268:
211:
210:
207:
206:
201:
195:
194:
189:
183:
182:
177:
171:
170:
162:
161:
152:
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:
1918:
1907:
1904:
1902:
1899:
1897:
1894:
1893:
1891:
1881:
1876:
1871:
1867:
1853:
1849:
1848:
1843:
1840:
1836:
1835:
1830:
1827:
1823:
1822:
1817:
1814:
1810:
1809:
1804:
1801:
1797:
1796:
1791:
1788:
1784:
1783:
1778:
1775:
1771:
1770:
1765:
1764:
1762:
1758:
1752:
1749:
1747:
1744:
1742:
1739:
1737:
1734:
1732:
1729:
1728:
1726:
1722:
1716:
1713:
1711:
1710:Enzyme family
1708:
1706:
1703:
1701:
1698:
1697:
1695:
1691:
1685:
1682:
1680:
1677:
1675:
1674:Cooperativity
1672:
1670:
1667:
1666:
1664:
1660:
1654:
1651:
1649:
1646:
1644:
1641:
1639:
1636:
1634:
1633:Oxyanion hole
1631:
1629:
1626:
1624:
1621:
1619:
1616:
1615:
1613:
1609:
1605:
1598:
1593:
1591:
1586:
1584:
1579:
1578:
1575:
1563:
1560:
1558:
1555:
1554:
1552:
1548:
1542:
1539:
1538:
1536:
1533:
1529:
1525:
1519:
1516:
1514:
1511:
1509:
1506:
1505:
1503:
1500:
1496:
1492:
1486:
1483:
1481:
1478:
1476:
1473:
1472:
1470:
1467:
1463:
1459:
1455:
1450:
1446:
1439:
1434:
1432:
1427:
1425:
1420:
1419:
1416:
1405:
1401:
1397:
1393:
1389:
1385:
1381:
1374:
1371:
1366:
1362:
1357:
1352:
1349:(2): 1471–8.
1348:
1344:
1343:J. Biol. Chem
1340:
1333:
1330:
1325:
1321:
1316:
1311:
1306:
1301:
1298:(3): 985–97.
1297:
1293:
1289:
1282:
1279:
1274:
1270:
1265:
1260:
1256:
1252:
1248:
1244:
1240:
1236:
1232:
1225:
1222:
1217:
1213:
1208:
1203:
1199:
1195:
1191:
1187:
1183:
1179:
1175:
1160:
1157:
1152:
1148:
1143:
1138:
1134:
1130:
1126:
1122:
1118:
1111:
1108:
1103:
1099:
1095:
1091:
1087:
1083:
1076:
1073:
1068:
1064:
1060:
1056:
1052:
1048:
1044:
1040:
1033:
1030:
1025:
1021:
1016:
1011:
1007:
1003:
999:
995:
991:
984:
981:
976:
972:
967:
962:
958:
954:
953:J. Biol. Chem
950:
943:
940:
935:
931:
926:
921:
916:
911:
907:
903:
902:J. Biol. Chem
899:
892:
890:
888:
884:
879:
875:
871:
867:
863:
859:
852:
850:
848:
846:
842:
837:
833:
829:
825:
821:
817:
813:
809:
802:
799:
794:
790:
786:
782:
778:
774:
767:
764:
759:
755:
751:
747:
743:
739:
735:
731:
727:
725:
716:
713:
708:
704:
699:
694:
689:
684:
680:
676:
672:
665:
662:
655:
653:
651:
646:
642:
638:
634:
626:
624:
622:
621:metronidazole
618:
605:
600:
598:
594:
590:
589:methemoglobin
586:
582:
577:
575:
571:
567:
563:
559:
555:
551:
547:
539:
537:
535:
531:
527:
523:
519:
515:
511:
507:
502:
490:
485:
478:
473:
468:
466:
463:
459:
455:
451:
447:
443:
439:
438:binding sites
435:
431:
426:
414:
409:
402:
397:
390:
385:
380:
378:
376:
372:
368:
364:
360:
356:
352:
348:
344:
340:
336:
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328:
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316:
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307:
305:
301:
297:
293:
289:
285:
280:
257:
256:
252:
248:
244:
241:
237:
233:
228:
226:
225:methemoglobin
222:
217:
205:
202:
200:
196:
193:
190:
188:
184:
181:
178:
176:
172:
167:
163:
160:
156:
153:
151:
150:Gene Ontology
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:
1847:Translocases
1844:
1831:
1818:
1805:
1792:
1782:Transferases
1779:
1766:
1623:Binding site
1390:(1): 76–81.
1387:
1383:
1373:
1346:
1342:
1332:
1295:
1291:
1281:
1238:
1234:
1224:
1181:
1177:
1159:
1127:(2): 385–7.
1124:
1120:
1110:
1085:
1082:Biochemistry
1081:
1075:
1045:(1): 53–64.
1042:
1038:
1032:
997:
993:
983:
956:
952:
942:
905:
901:
861:
858:Biochemistry
857:
811:
807:
801:
776:
772:
766:
733:
729:
723:
715:
678:
674:
664:
650:carcinogenic
644:
630:
601:
593:erythrocytes
578:
569:
561:
557:
543:
498:
422:
374:
370:
366:
362:
358:
354:
350:
346:
342:
338:
334:
330:
326:
322:
318:
308:
281:
258:
235:
229:
215:
214:
76:BRENDA entry
1618:Active site
558:P. fischeri
526:protonation
430:hydrophobic
64:IntEnz view
47:56626-29-0
24:Identifiers
1890:Categories
1821:Isomerases
1795:Hydrolases
1662:Regulation
1121:Biochem. J
1015:2297/36899
814:(1): 3–8.
773:J. Biochem
656:References
633:carcinomas
562:B. harveyi
554:luciferase
458:amino acid
440:, one for
296:riboflavin
292:substrates
232:enzymology
133:structures
100:KEGG entry
1700:EC number
1447:: CH-NH (
1380:Kramer DM
1255:0950-382X
1000:: 143–8.
808:Biometals
581:catalyzes
546:organisms
501:mechanism
469:Mechanism
450:reduction
267:⇌
251:catalyzes
53:Databases
1896:EC 1.5.1
1724:Kinetics
1648:Cofactor
1611:Activity
1534:acceptor
1501:acceptor
1468:acceptor
1404:12054743
1365:10625700
1324:24202330
1273:24256032
1216:24487531
1102:24004065
1067:21243671
1024:24529496
934:22052907
836:10007595
758:15295145
750:24190498
707:24567729
595:and the
574:bacteria
550:luminous
522:Nitrogen
436:has two
284:products
245:) is an
243:1.5.1.30
204:proteins
192:articles
180:articles
137:RCSB PDB
35:1.5.1.30
1880:Biology
1834:Ligases
1604:Enzymes
1532:quinone
1315:3795375
1264:4437529
1207:3993133
1186:Bibcode
1151:8687377
1142:1217361
975:8530465
925:3243531
878:8885832
828:8118169
793:7400118
724:E. coli
698:3915288
570:in vivo
564:cells,
514:sterics
510:hydride
221:flavins
159:QuickGO
124:profile
107:MetaCyc
42:CAS no.
1866:Portal
1808:Lyases
1550:1.5.99
1499:oxygen
1402:
1363:
1322:
1312:
1271:
1261:
1253:
1214:
1204:
1149:
1139:
1100:
1065:
1057:
1022:
973:
932:
922:
876:
834:
826:
791:
756:
748:
705:
695:
681:: 25.
637:tumors
434:enzyme
373:, and
302:, and
247:enzyme
187:PubMed
169:Search
155:AmiGO
143:PDBsum
83:ExPASy
71:BRENDA
59:IntEnz
30:EC no.
1760:Types
1528:1.5.5
1495:1.5.3
1458:1.5.1
1063:S2CID
1059:47604
832:S2CID
754:S2CID
635:, or
597:liver
585:NADPH
530:NADPH
518:NADP+
506:NADPH
442:NADPH
425:dimer
300:NADPH
249:that
119:PRIAM
1852:list
1845:EC7
1839:list
1832:EC6
1826:list
1819:EC5
1813:list
1806:EC4
1800:list
1793:EC3
1787:list
1780:EC2
1774:list
1767:EC1
1466:NADP
1451:1.5)
1400:PMID
1361:PMID
1320:PMID
1269:PMID
1251:ISSN
1212:PMID
1147:PMID
1098:PMID
1055:PMID
1020:PMID
971:PMID
930:PMID
874:PMID
824:PMID
789:PMID
746:PMID
703:PMID
560:and
534:NADH
499:The
294:are
288:NADP
253:the
234:, a
199:NCBI
140:PDBe
95:KEGG
1464:or
1462:NAD
1392:doi
1388:294
1351:doi
1347:275
1310:PMC
1300:doi
1259:PMC
1243:doi
1202:PMC
1194:doi
1137:PMC
1129:doi
1125:316
1090:doi
1047:doi
1010:hdl
1002:doi
961:doi
957:270
920:PMC
910:doi
906:286
866:doi
816:doi
781:doi
738:doi
693:PMC
683:doi
591:in
583:an
462:FAD
230:In
175:PMC
131:PDB
1892::
1530::
1497::
1460::
1449:EC
1398:.
1386:.
1359:.
1345:.
1341:.
1318:.
1308:.
1294:.
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1257:.
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1239:91
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1192:.
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1180:.
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1145:.
1135:.
1123:.
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1084:.
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1008:.
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900:.
886:^
872:.
862:35
860:.
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830:.
822:.
810:.
787:.
777:87
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752:.
744:.
734:98
732:.
728:.
701:.
691:.
677:.
673:.
599:.
536:.
377:.
369:,
365:,
361:,
357:,
353:,
349:,
345:,
341:,
337:,
333:,
329:,
325:,
306:.
298:,
240:EC
157:/
1868::
1854:)
1850:(
1841:)
1837:(
1828:)
1824:(
1815:)
1811:(
1802:)
1798:(
1789:)
1785:(
1776:)
1772:(
1596:e
1589:t
1582:v
1437:e
1430:t
1423:v
1406:.
1394::
1367:.
1353::
1326:.
1302::
1296:5
1275:.
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1218:.
1196::
1188::
1172:2
1170:O
1168:2
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1131::
1104:.
1092::
1069:.
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1043:6
1026:.
1012::
1004::
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963::
936:.
912::
880:.
868::
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812:7
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760:.
740::
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709:.
685::
679:5
612:2
610:O
608:2
304:H
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