29:
581:
2784:
33:
Structure of the kynurenine 3-monooxygenase dimer, generated from 4J34. One monomer is depicted in cartoon format (cyan) and the second monomer is displayed in ribbon format (green). The flexible linker regions (residues 96-104) are colored red. Flavin adenine dinucleotide (FAD) is shown as spheres
400:
with the human kynurenine 3-monooxygenase protein. Studies have shown the beneficial effects of enzyme inhibition in these eukaryotic kynurenine 3-monooxygenase active sites, thus making this enzyme an attractive target for human drug design.
687:. Administration of potent enzyme inhibitors has demonstrated promising pharmacological results. Specifically, genetic elimination of the kynurenine 3-monooxygenase enzyme has been shown to suppress toxicity of the
443:-kynurenine, structural studies of the enzyme in yeast co-crystallized with UPF 648 reveal how the FAD cofactor and substrate are bound in the active site. Chemical similarities between UPF 648 and
667:
at the glycine site of the NMDA receptor. As a result, regulation at the kynurenine 3-monooxygenase enzyme determines the neurotoxic and neuroprotective potential of the kynurenine pathway.
417:
and has one FAD-binding domain as its prosthetic group. Kynurenine 3-monooxygenase contains a linker region involved in substrate binding following a second strand of an antiparallel
195:
537:-kynurenine with concomitant interconversion of NADPH to NADP. The reaction mechanism is not entirely known, but is believed to follow mechanisms related to the
1447:"The brain metabolite kynurenic acid inhibits α7 nicotinic receptor activity and increases non-α7 nicotinic receptor expression:Physiopathological implications"
214:
1146:: substrate-like inhibitors both stimulate flavin reduction and stabilize the flavin-peroxo intermediate yet result in the production of hydrogen peroxide".
295:
270:
1643:"Downregulated Kynurenine 3-Monooxygenase Gene Expression and Enzyme Activity in Schizophrenia and Genetic Association With Schizophrenia Endophenotypes"
850:
Smith, Jason R.; Jamie, Joanne F.; Guillemin, Gilles J. (February 2016). "Kynurenine-3-monooxygenase: a review of structure, mechanism, and inhibitors".
652:
subtype of glutamate receptors, producing excitotoxic lesions in the central nervous system of mammals. Quinolinic acid is also the bioprecursor of NAD.
724:
in kynurenine 3-monooxygenase-deficient patients results in a shift towards kynurenic acid production, believed to be related to cognitive deficits in
2261:
2154:
1933:
Foucher AL, McIntosh A, Douce G, Wastling J, Tait A, Turner CM (2006). "A proteomic analysis of arsenical drug resistance in
Trypanosoma brucei".
362:
as the oxidant. Kynurenine 3-monooxygenase catalyzes the insertion of molecular oxygen into the aromatic ring of kynurenine to produce 3-hydroxy-
2329:
2068:
376:. Kynurenine 3-monooxygenase serves as an important branch point in the kynurenine pathway and, as a result, is an attractive drug target for
819:
553:-kynurenine-FAD-hydroperoxide intermediate. This intermediate is the electrophilic source for the hydroxylation reaction, yielding a primary
655:
Inhibition of kynurenine 3-monooxygenase leads to an increase of kynurenic acid in the kynurenine pathway. This metabolite functions as an
2819:
2229:
1269:"Targeted Deletion of Kynurenine 3-Monooxygenase in Mice: A New Tool for Studying Kynurenine Pathway Metabolism in Periphery and Brain"
1229:
Thevandavakkam MA, et al. (2010). "Targeting kynurenine 3-monooxygenase (KMO). Implications for therapy in
Huntington's disease".
1692:"Kynurenine 3-monooxygenase polymorphisms: relevance for kynurenic acid synthesis in patients with schizophrenia and healthy controls"
2503:
2202:
1545:
Campesan, S.; Green, E. W.; Breda, C.; Sathyasaikumar, K. V.; Muchowski, P. J.; Schwarcz, R.; Kyriacou, C. P.; Giorgini, F (2011).
207:
2809:
675:
Kynurenine 3-monooxygenase is an attractive drug target for several neurodegenerative and neuroinflammatory diseases, especially
584:
The mechanism of kynurenine 3-monooxygenase FAD is shown in blue. The substrate, intermediate, and product are depicted in black.
2241:
2187:
538:
1970:
Okamoto H, Hayaishi O (1967). "Flavin adenine dinucleotide requirement for kynurenine hydroxylase of rat liver mitochondria".
158:
134:
2659:
802:
Filippini, Graziella
Allegri; Costa, Carlo V. L.; Bertazzo, Antonella; International Meeting on Tryptophan Research (1998).
2046:
2774:
762:
Amaral, M. (2014). "Crystal
Structure of kynurenine 3-monooxygenase – truncated at position 394 plus HIS tag cleaved".
2470:
2319:
373:
1361:
Stone, T. W.; Perkins, M. N. (1981). "Quinolinic acid: A potent endogenous excitant at amino acid receptors in CNS".
2061:
660:
2644:
1790:
Hoekstra, PJ; Anderson, GM; Troost, PW (2007). "Plasma kynurenine and related measures in tic disorder patients".
2760:
2747:
2734:
2721:
2708:
2695:
2682:
2465:
2426:
2416:
2402:
2398:
2388:
2376:
2356:
2339:
2307:
2271:
2171:
2098:
152:
2654:
1498:"A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease"
2608:
2551:
2089:
240:
45:
2311:
1051:"Kynurenine-3-monooxygenase inhibition prevents multiple organ failure in rodent models of acute pancreatitis"
139:
2556:
2102:
676:
369:
1892:
Yukiko, Hirata; Takashi, Kawachi; Takashi, Sugimura (2 October 1967). "Fatty liver induced by injection of
2814:
2450:
2366:
2115:
1835:"Identification of Metabolites, Clinical Chemistry Markers and Transcripts Associated with Hepatotoxicity"
1318:
Rios, C.; Santamaria, A. (1991). "Quinolinic acid is a potent lipid peroxidant in rat brain homogenates".
701:
684:
680:
219:
28:
127:
2577:
2496:
2246:
2219:
2054:
775:
344:
2649:
2361:
2324:
2085:
1846:
964:
62:
1445:
Hilmas, C.; Pereira, E. F.; Alkondon, M.; Rassoulpour, A.; Schwarcz, R.; Albuquerque, E. X. (2001).
437:
While no scientific literature reports a crystal image of a kynurenine 3-monooxygenase complex with
155:
2804:
2613:
2347:
1100:"Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase"
656:
285:
79:
57:
951:
Amaral, M; Levy, C; Heyes, DJ; Lafite, P; Outeiro, TF; Giorgini, F; Leys, D; Scrutton, NS (2013).
388:. Currently, most research on the kynurenine 3-monooxygenase enzyme has been focused primarily on
2546:
2110:
1958:
1815:
1623:
1343:
825:
606:
397:
348:
2256:
2144:
2034:
1987:
1950:
1915:
1874:
1807:
1772:
1721:
1672:
1615:
1580:
1527:
1478:
1427:
1378:
1335:
1300:
1246:
1211:
1163:
1121:
1080:
1031:
990:
916:
875:
867:
815:
713:
429:
C-terminus acts as the mitochondrial anchoring domain and participates in enzymatic activity.
385:
381:
255:
146:
619:-Kynurenine is an important branch point of this metabolic pathway, being converted into the
2592:
2587:
2561:
2489:
2024:
1979:
1942:
1907:
1864:
1854:
1799:
1762:
1752:
1711:
1703:
1662:
1654:
1607:
1570:
1562:
1517:
1509:
1468:
1458:
1417:
1409:
1370:
1327:
1290:
1280:
1238:
1201:
1155:
1111:
1070:
1062:
1023:
980:
972:
908:
859:
807:
763:
717:
634:
115:
2639:
2623:
2536:
2234:
788:
645:
547:-kynurenine binds, NADPH reduces FAD and leaves as NADP. Oxygen then binds and creates an
414:
314:
91:
563:-kynurenine in complex with the enzyme (E Fl HOH-P). Dissociation of 3-hydroxy-
513:
also form polar contacts with the carboxylate in the amino acid moiety on the substrate.
464:
is believed to be the oxygen-binding site above the re-side of the FAD prosthetic group.
50:
1850:
968:
732:. Kynurenine-3-monooxygenase deficiency is associated with disorders of the brain (e.g.
2788:
2677:
2618:
2460:
2440:
2435:
2077:
1869:
1834:
1767:
1740:
1716:
1691:
1667:
1642:
1575:
1546:
1522:
1497:
1473:
1463:
1446:
1422:
1397:
1295:
1268:
1075:
1050:
985:
952:
729:
725:
630:
580:
352:
190:
2029:
2000:
1658:
1206:
1185:
1008:
Hirai KH, et al. (2010). "Dual role of the carboxyl-terminal region of pig liver
170:
2798:
2582:
2541:
1983:
1911:
1374:
1116:
1099:
1014:-kynurenine 3-monooxygenase: mitochondrial-targeting signal and enzymatic activity".
893:
Horn, U.; Ullrich, V.; Staudinger, H.J (1971). "Purification and characterization of
737:
733:
649:
522:
410:
165:
1962:
1819:
1598:
MĂĽller, N; Myint, AM; Schwarz, MJ (2010). "Inflammatory
Biomarkers and Depression".
1347:
829:
2531:
2279:
2275:
1627:
638:
450:
274:
1859:
1496:
Giorgini, F.; Guidetti, P.; Nguyen, Q.; Bennett, S. C.; Muchowski, P. J. (2005).
912:
863:
2755:
2690:
2526:
422:
174:
2783:
1242:
804:
Recent advances in tryptophan research : tryptophan and serotonin pathways
2411:
1803:
1611:
1566:
811:
721:
709:
693:
688:
664:
620:
610:
557:
form of the product and the C4a-hydroxy-FAD. Tautomerization yields 3-hydroxy-
505:-kynurenine carbonyl group, as well as on the hydrogen on the FAD N3 atom. Arg
426:
418:
377:
310:
261:
232:
1757:
871:
495:) positioned around the substrate's aromatic benzene moiety. A conserved Gln
2729:
2703:
2380:
2343:
2287:
2081:
1285:
705:
389:
251:
2038:
1954:
1946:
1878:
1811:
1776:
1725:
1676:
1619:
1584:
1531:
1482:
1431:
1304:
1250:
1167:
1125:
1084:
1035:
994:
879:
1991:
1919:
1382:
1339:
920:
767:
2159:
1215:
243:
103:
1739:
Campbell, Brian M.; Charych, Erik; Lee, Anna W.; Möller, Thomas (2014).
1142:
Crozier-Reabe, KR; et al. (2008). "Kynurenine 3-monooxygenase from
1027:
976:
2455:
1707:
1331:
122:
1159:
700:
Kynurenine 3-monooxygenase deficiency, which can be caused by genetic
2742:
2512:
2297:
2292:
2251:
1833:
Buness A, Roth A, Herrmann A, Schmitz O, Kamp H, et al. (2014).
1398:"Kynurenines in the mammalian brain. When physiology meets pathology"
356:
278:
247:
202:
98:
86:
74:
1413:
1066:
1513:
720:. Recent research suggests that hyperphysiologic concentrations of
2716:
2444:
2179:
2137:
2130:
2125:
2120:
644:
Kynurenine 3-monooxygenase regulates the downstream production of
579:
554:
467:
Each monomer contains a conserved hydrophobic pocket (residues Leu
393:
299:
1900:
Biochimica et
Biophysica Acta (BBA) - Lipids and Lipid Metabolism
1741:"Kynurenines in CNS disease: regulation byinflammatory cytokines"
2224:
2212:
2207:
2197:
2192:
2175:
2149:
1641:
Wonodi I, Colin-Stine O, Sathyasaikumar KV, et al. (2011).
1396:
Schwarcz, R.; Bruno, J. P.; Muchowski, P. J.; Wu, H. Q. (2012).
806:. Advances in Experimental Medicine and Biology. Vol. 398.
629:-kynurenine via kynurenine 3-monooxygenase, the neuroprotectant
110:
2485:
2050:
648:, which can generate reactive free radicals and activates the
1267:
Giorgini F, Huang SY, Sathyasaikumar KV, et al. (2013).
449:-kynurenine suggest that the substrate binds adjacent to the
396:, both of which have been demonstrated to have high sequence
1186:"Flavin-oxygen derivatives involved in the hydroxylation of
309:
Kynurenine 3-monooxygenase is the expression product of the
953:"Structural basis of kynurenine 3-monooxygenase inhibition"
2481:
899:-kynurenine 3-hydroxylase (EC 1.14.1.2.) from rat liver".
757:
755:
753:
499:
polar residue is also involved in hydrogen bonding on the
324:-kynurenine, NADPH:oxygen oxidoreductase (3-hydroxylating)
2001:"Studies on oxygenases; enzymatic formation of 3-hydroxy-
1547:"The kynurenine pathway modulates neurodegeneration in a
609:. The kynurenine pathway is responsible for over 95% of
593:
Kynurenine 3-monooxygenase catalyzes the conversion of
456:
of the flavoprotein. A loop containing the residues Pro
605:-kynurenine, an important bioactive metabolite in the
355:, to be specific, those acting on paired donors, with
2772:
1137:
1135:
421:, a six-stranded antiparallel β-sheet domain, and an
2668:
2632:
2601:
2570:
2519:
2425:
2397:
2375:
2338:
2306:
2270:
2170:
2097:
1690:Holtze M, Saetre P, Engberg G, et al. (2012).
213:
201:
189:
184:
164:
145:
133:
121:
109:
97:
85:
73:
68:
56:
44:
39:
21:
1262:
1260:
1179:
1177:
946:
944:
942:
940:
938:
936:
934:
932:
930:
2497:
2062:
845:
843:
841:
839:
8:
2504:
2490:
2482:
2069:
2055:
2047:
633:through kynurenine amino transferases, or
181:
27:
2028:
1868:
1858:
1766:
1756:
1715:
1666:
1574:
1521:
1472:
1462:
1421:
1294:
1284:
1205:
1115:
1074:
984:
521:Kynurenine-3-monooxygenase catalyzes the
1999:Saito Y, Hayaishi O, Rothberg S (1957).
2779:
749:
708:, or both, leads to an accumulation of
351:. This enzyme belongs to the family of
784:
773:
18:
712:and to a shift within the tryptophan
573:O leads to the free enzyme (E Fl
7:
2262:24-hydroxycholesterol 7α-hydroxylase
326:. Other names in common use include
1273:The Journal of Biological Chemistry
661:α7 nicotinic acetylcholine receptor
34:color-coded according to atom type.
1464:10.1523/JNEUROSCI.21-19-07463.2001
14:
1659:10.1001/archgenpsychiatry.2011.71
2782:
1231:CNS Neurol. Disord. Drug Targets
1117:10.1046/j.1432-1327.2000.01104.x
1098:Breton, J.; et al. (2000).
697:models of Huntington's disease.
409:Kynurenine 3-monooxygenase is a
2242:Cholesterol 7 alpha-hydroxylase
2188:Flavin-containing monooxygenase
901:Hoppe-Seyler's Z. Physiol. Chem
539:flavin-dependent monooxygenases
1551:model of Huntington's disease"
1184:Entsch B, et al. (1976).
1:
2030:10.1016/S0021-9258(19)63696-3
1972:Biochem. Biophys. Res. Commun
1207:10.1016/S0021-9258(17)33523-8
1190:-hydroxybenzoate hydroxylase"
425:at the carboxy-terminal. The
1984:10.1016/0006-291X(67)90469-X
1912:10.1016/0005-2760(67)90153-1
1860:10.1371/journal.pone.0097249
1792:Eur Child Adolesc Psychiatry
1375:10.1016/0014-2999(81)90587-2
1049:Mole D, et al. (2016).
913:10.1515/bchm2.1971.352.1.837
864:10.1016/j.drudis.2015.11.001
368:-kynurenine. It employs one
349:kynurenine catabolic pathway
2471:Deoxyhypusine monooxygenase
730:visuospatial working memory
716:towards kynurenic acid and
2836:
2820:Enzymes of known structure
1243:10.2174/187152710793237430
386:neuroinflammatory diseases
237:kynurenine 3-monooxygenase
22:kynurenine 3-monooxygenase
2660:Michaelis–Menten kinetics
2466:Ecdysone 20-monooxygenase
2417:Stearoyl-CoA desaturase-1
2389:Dopamine beta-hydroxylase
2357:Phenylalanine hydroxylase
1804:10.1007/s00787-007-1009-1
1745:Frontiers in Neuroscience
1612:10.1007/s12640-010-9210-2
1567:10.1016/j.cub.2011.04.028
812:10.1007/978-1-4613-0381-7
599:-kynurenine to 3-hydroxy-
531:-kynurenine to 3-hydroxy-
341:-kynurenine-3-hydroxylase
180:
26:
2552:Diffusion-limited enzyme
1758:10.3389/fnins.2014.00012
328:kynurenine 3-hydroxylase
317:of this enzyme class is
2810:NADPH-dependent enzymes
1286:10.1074/jbc.M113.503813
1144:Pseudomonas fluorescens
613:oxidative degradation.
2451:Squalene monooxygenase
2367:Tryptophan hydroxylase
2116:HIF prolyl-hydroxylase
1947:10.1002/pmic.200500419
783:Cite journal requires
585:
413:containing asymmetric
343:. It participates in
332:kynurenine hydroxylase
2645:Eadie–Hofstee diagram
2578:Allosteric regulation
2247:Methane monooxygenase
2220:Nitric oxide synthase
1696:J Psychiatry Neurosci
691:protein in yeast and
583:
345:tryptophan metabolism
2655:Lineweaver–Burk plot
2362:Tyrosine hydroxylase
2086:steroid hydroxylases
852:Drug Discovery Today
740:) and of the liver.
2312:iron–sulfur protein
1851:2014PLoSO...997249B
1647:Arch Gen Psychiatry
1279:(51): 36554–36566.
1154:(47): 12420–12433.
977:10.1038/nature12039
969:2013Natur.496..382A
768:10.2210/pdb4j34/pdb
685:Parkinson's disease
589:Biological function
2614:Enzyme superfamily
2547:Enzyme promiscuity
2111:Prolyl hydroxylase
1798:(Suppl 1): 71–77.
1708:10.1503/jpn.100175
1402:Nat. Rev. Neurosci
1332:10.1007/bf00966592
726:predictive pursuit
607:kynurenine pathway
586:
2770:
2769:
2479:
2478:
2145:Lysyl hydroxylase
2007:-kynurenine from
1457:(19): 7463–7473.
1363:Eur. J. Pharmacol
1326:(10): 1139–1143.
1160:10.1021/bi8010434
1028:10.1093/jb/mvq099
963:(7445): 382–385.
821:978-1-4613-8026-9
714:metabolic pathway
671:Disease relevance
569:-kynurenine and H
382:neurodegenerative
256:chemical reaction
229:
228:
225:
224:
128:metabolic pathway
2827:
2787:
2786:
2778:
2650:Hanes–Woolf plot
2593:Enzyme activator
2588:Enzyme inhibitor
2562:Enzyme catalysis
2506:
2499:
2492:
2483:
2071:
2064:
2057:
2048:
2042:
2032:
2012:
2011:
2006:
2005:
1995:
1966:
1941:(9): 2726–2732.
1924:
1923:
1897:
1896:
1889:
1883:
1882:
1872:
1862:
1830:
1824:
1823:
1787:
1781:
1780:
1770:
1760:
1736:
1730:
1729:
1719:
1687:
1681:
1680:
1670:
1638:
1632:
1631:
1595:
1589:
1588:
1578:
1542:
1536:
1535:
1525:
1493:
1487:
1486:
1476:
1466:
1442:
1436:
1435:
1425:
1393:
1387:
1386:
1358:
1352:
1351:
1315:
1309:
1308:
1298:
1288:
1264:
1255:
1254:
1226:
1220:
1219:
1209:
1200:(9): 2550–2563.
1181:
1172:
1171:
1139:
1130:
1129:
1119:
1110:(4): 1092–1099.
1095:
1089:
1088:
1078:
1046:
1040:
1039:
1013:
1012:
1005:
999:
998:
988:
948:
925:
924:
898:
897:
890:
884:
883:
847:
834:
833:
799:
793:
792:
786:
781:
779:
771:
759:
718:anthranilic acid
635:anthranilic acid
628:
627:
618:
617:
604:
603:
598:
597:
568:
567:
562:
561:
552:
551:
546:
545:
536:
535:
530:
529:
504:
503:
448:
447:
442:
441:
367:
366:
340:
339:
323:
322:
291:
290:
266:
265:
182:
31:
19:
2835:
2834:
2830:
2829:
2828:
2826:
2825:
2824:
2795:
2794:
2793:
2781:
2773:
2771:
2766:
2678:Oxidoreductases
2664:
2640:Enzyme kinetics
2628:
2624:List of enzymes
2597:
2566:
2537:Catalytic triad
2515:
2510:
2480:
2475:
2429:- miscellaneous
2421:
2393:
2371:
2334:
2302:
2266:
2257:14α-demethylase
2166:
2093:
2078:Oxidoreductases
2075:
2045:
2009:
2008:
2003:
2002:
1998:
1969:
1932:
1928:
1927:
1894:
1893:
1891:
1890:
1886:
1832:
1831:
1827:
1789:
1788:
1784:
1738:
1737:
1733:
1689:
1688:
1684:
1640:
1639:
1635:
1597:
1596:
1592:
1561:(11): 961–966.
1544:
1543:
1539:
1495:
1494:
1490:
1444:
1443:
1439:
1414:10.1038/nrn3257
1395:
1394:
1390:
1360:
1359:
1355:
1317:
1316:
1312:
1266:
1265:
1258:
1228:
1227:
1223:
1183:
1182:
1175:
1141:
1140:
1133:
1104:Eur. J. Biochem
1097:
1096:
1092:
1067:10.1038/nm.4020
1055:Nature Medicine
1048:
1047:
1043:
1010:
1009:
1007:
1006:
1002:
950:
949:
928:
895:
894:
892:
891:
887:
849:
848:
837:
822:
801:
800:
796:
782:
772:
761:
760:
751:
746:
673:
646:quinolinic acid
625:
624:
615:
614:
601:
600:
595:
594:
591:
576:
572:
565:
564:
559:
558:
549:
548:
543:
542:
533:
532:
527:
526:
519:
512:
508:
501:
500:
498:
494:
490:
486:
482:
478:
474:
470:
463:
459:
445:
444:
439:
438:
435:
407:
364:
363:
360:
353:oxidoreductases
337:
336:
320:
319:
315:systematic name
303:
288:
287:
282:
263:
262:
35:
17:
12:
11:
5:
2833:
2831:
2823:
2822:
2817:
2812:
2807:
2797:
2796:
2792:
2791:
2768:
2767:
2765:
2764:
2751:
2738:
2725:
2712:
2699:
2686:
2672:
2670:
2666:
2665:
2663:
2662:
2657:
2652:
2647:
2642:
2636:
2634:
2630:
2629:
2627:
2626:
2621:
2616:
2611:
2605:
2603:
2602:Classification
2599:
2598:
2596:
2595:
2590:
2585:
2580:
2574:
2572:
2568:
2567:
2565:
2564:
2559:
2554:
2549:
2544:
2539:
2534:
2529:
2523:
2521:
2517:
2516:
2511:
2509:
2508:
2501:
2494:
2486:
2477:
2476:
2474:
2473:
2468:
2463:
2458:
2453:
2448:
2441:Heme oxygenase
2438:
2436:Cyclooxygenase
2432:
2430:
2423:
2422:
2420:
2419:
2414:
2408:
2406:
2395:
2394:
2392:
2391:
2385:
2383:
2373:
2372:
2370:
2369:
2364:
2359:
2353:
2351:
2336:
2335:
2333:
2332:
2327:
2322:
2316:
2314:
2304:
2303:
2301:
2300:
2295:
2290:
2284:
2282:
2268:
2267:
2265:
2264:
2259:
2254:
2249:
2244:
2239:
2238:
2237:
2232:
2227:
2217:
2216:
2215:
2210:
2205:
2200:
2195:
2184:
2182:
2168:
2167:
2165:
2164:
2163:
2162:
2157:
2147:
2142:
2141:
2140:
2135:
2134:
2133:
2128:
2123:
2107:
2105:
2103:2-oxoglutarate
2095:
2094:
2076:
2074:
2073:
2066:
2059:
2051:
2044:
2043:
2023:(2): 921–934.
1996:
1978:(3): 394–399.
1967:
1929:
1926:
1925:
1906:(2): 233–241.
1898:-tryptophan".
1884:
1825:
1782:
1731:
1682:
1653:(7): 665–674.
1633:
1606:(2): 308–318.
1590:
1537:
1514:10.1038/ng1542
1508:(5): 526–531.
1488:
1437:
1408:(7): 465–477.
1388:
1369:(4): 411–412.
1353:
1320:Neurochem. Res
1310:
1256:
1237:(6): 791–800.
1221:
1173:
1131:
1090:
1061:(2): 202–209.
1041:
1022:(6): 639–650.
1000:
926:
907:(6): 837–842.
885:
858:(2): 315–324.
835:
820:
794:
785:|journal=
748:
747:
745:
742:
672:
669:
631:kynurenic acid
590:
587:
574:
570:
518:
515:
510:
506:
496:
492:
488:
484:
480:
476:
472:
468:
461:
457:
434:
431:
406:
403:
392:models and in
358:
307:
306:
301:
280:
227:
226:
223:
222:
217:
211:
210:
205:
199:
198:
193:
187:
186:
178:
177:
168:
162:
161:
150:
143:
142:
137:
131:
130:
125:
119:
118:
113:
107:
106:
101:
95:
94:
89:
83:
82:
77:
71:
70:
66:
65:
60:
54:
53:
48:
42:
41:
37:
36:
32:
24:
23:
15:
13:
10:
9:
6:
4:
3:
2:
2832:
2821:
2818:
2816:
2815:Flavoproteins
2813:
2811:
2808:
2806:
2803:
2802:
2800:
2790:
2785:
2780:
2776:
2762:
2758:
2757:
2752:
2749:
2745:
2744:
2739:
2736:
2732:
2731:
2726:
2723:
2719:
2718:
2713:
2710:
2706:
2705:
2700:
2697:
2693:
2692:
2687:
2684:
2680:
2679:
2674:
2673:
2671:
2667:
2661:
2658:
2656:
2653:
2651:
2648:
2646:
2643:
2641:
2638:
2637:
2635:
2631:
2625:
2622:
2620:
2619:Enzyme family
2617:
2615:
2612:
2610:
2607:
2606:
2604:
2600:
2594:
2591:
2589:
2586:
2584:
2583:Cooperativity
2581:
2579:
2576:
2575:
2573:
2569:
2563:
2560:
2558:
2555:
2553:
2550:
2548:
2545:
2543:
2542:Oxyanion hole
2540:
2538:
2535:
2533:
2530:
2528:
2525:
2524:
2522:
2518:
2514:
2507:
2502:
2500:
2495:
2493:
2488:
2487:
2484:
2472:
2469:
2467:
2464:
2462:
2459:
2457:
2454:
2452:
2449:
2446:
2442:
2439:
2437:
2434:
2433:
2431:
2428:
2424:
2418:
2415:
2413:
2410:
2409:
2407:
2404:
2400:
2396:
2390:
2387:
2386:
2384:
2382:
2378:
2374:
2368:
2365:
2363:
2360:
2358:
2355:
2354:
2352:
2349:
2348:BH4 dependent
2345:
2341:
2337:
2331:
2328:
2326:
2323:
2321:
2318:
2317:
2315:
2313:
2309:
2305:
2299:
2296:
2294:
2291:
2289:
2286:
2285:
2283:
2281:
2277:
2273:
2269:
2263:
2260:
2258:
2255:
2253:
2250:
2248:
2245:
2243:
2240:
2236:
2233:
2231:
2228:
2226:
2223:
2222:
2221:
2218:
2214:
2211:
2209:
2206:
2204:
2201:
2199:
2196:
2194:
2191:
2190:
2189:
2186:
2185:
2183:
2181:
2177:
2173:
2169:
2161:
2158:
2156:
2153:
2152:
2151:
2148:
2146:
2143:
2139:
2136:
2132:
2129:
2127:
2124:
2122:
2119:
2118:
2117:
2114:
2113:
2112:
2109:
2108:
2106:
2104:
2100:
2096:
2091:
2087:
2083:
2079:
2072:
2067:
2065:
2060:
2058:
2053:
2052:
2049:
2040:
2036:
2031:
2026:
2022:
2018:
2017:J. Biol. Chem
2014:
1997:
1993:
1989:
1985:
1981:
1977:
1973:
1968:
1964:
1960:
1956:
1952:
1948:
1944:
1940:
1936:
1931:
1930:
1921:
1917:
1913:
1909:
1905:
1901:
1888:
1885:
1880:
1876:
1871:
1866:
1861:
1856:
1852:
1848:
1845:(5): e97249.
1844:
1840:
1836:
1829:
1826:
1821:
1817:
1813:
1809:
1805:
1801:
1797:
1793:
1786:
1783:
1778:
1774:
1769:
1764:
1759:
1754:
1750:
1746:
1742:
1735:
1732:
1727:
1723:
1718:
1713:
1709:
1705:
1701:
1697:
1693:
1686:
1683:
1678:
1674:
1669:
1664:
1660:
1656:
1652:
1648:
1644:
1637:
1634:
1629:
1625:
1621:
1617:
1613:
1609:
1605:
1601:
1600:Neurotox. Res
1594:
1591:
1586:
1582:
1577:
1572:
1568:
1564:
1560:
1556:
1552:
1550:
1541:
1538:
1533:
1529:
1524:
1519:
1515:
1511:
1507:
1503:
1499:
1492:
1489:
1484:
1480:
1475:
1470:
1465:
1460:
1456:
1452:
1448:
1441:
1438:
1433:
1429:
1424:
1419:
1415:
1411:
1407:
1403:
1399:
1392:
1389:
1384:
1380:
1376:
1372:
1368:
1364:
1357:
1354:
1349:
1345:
1341:
1337:
1333:
1329:
1325:
1321:
1314:
1311:
1306:
1302:
1297:
1292:
1287:
1282:
1278:
1274:
1270:
1263:
1261:
1257:
1252:
1248:
1244:
1240:
1236:
1232:
1225:
1222:
1217:
1213:
1208:
1203:
1199:
1195:
1194:J. Biol. Chem
1191:
1189:
1180:
1178:
1174:
1169:
1165:
1161:
1157:
1153:
1149:
1145:
1138:
1136:
1132:
1127:
1123:
1118:
1113:
1109:
1105:
1101:
1094:
1091:
1086:
1082:
1077:
1072:
1068:
1064:
1060:
1056:
1052:
1045:
1042:
1037:
1033:
1029:
1025:
1021:
1017:
1004:
1001:
996:
992:
987:
982:
978:
974:
970:
966:
962:
958:
954:
947:
945:
943:
941:
939:
937:
935:
933:
931:
927:
922:
918:
914:
910:
906:
902:
889:
886:
881:
877:
873:
869:
865:
861:
857:
853:
846:
844:
842:
840:
836:
831:
827:
823:
817:
813:
809:
805:
798:
795:
790:
777:
769:
765:
758:
756:
754:
750:
743:
741:
739:
738:tic disorders
735:
734:schizophrenia
731:
727:
723:
719:
715:
711:
707:
703:
702:polymorphisms
698:
696:
695:
690:
686:
682:
678:
670:
668:
666:
662:
658:
653:
651:
647:
642:
640:
636:
632:
622:
612:
608:
588:
582:
578:
556:
540:
524:
523:hydroxylation
516:
514:
465:
455:
453:
432:
430:
428:
424:
420:
416:
412:
404:
402:
399:
395:
391:
387:
383:
379:
378:immunological
375:
371:
361:
354:
350:
346:
342:
333:
329:
325:
316:
312:
305:
297:
293:
283:
276:
272:
268:
260:
259:
258:
257:
253:
249:
245:
242:
238:
234:
221:
218:
216:
212:
209:
206:
204:
200:
197:
194:
192:
188:
183:
179:
176:
172:
169:
167:
166:Gene Ontology
163:
160:
157:
154:
151:
148:
144:
141:
138:
136:
132:
129:
126:
124:
120:
117:
114:
112:
108:
105:
104:NiceZyme view
102:
100:
96:
93:
90:
88:
84:
81:
78:
76:
72:
67:
64:
61:
59:
55:
52:
49:
47:
43:
38:
30:
25:
20:
2756:Translocases
2753:
2740:
2727:
2714:
2701:
2691:Transferases
2688:
2675:
2532:Binding site
2280:flavoprotein
2084:, including
2082:dioxygenases
2020:
2016:
2013:-kynurenine"
1975:
1971:
1938:
1934:
1903:
1899:
1887:
1842:
1838:
1828:
1795:
1791:
1785:
1748:
1744:
1734:
1702:(1): 53–57.
1699:
1695:
1685:
1650:
1646:
1636:
1603:
1599:
1593:
1558:
1554:
1548:
1540:
1505:
1501:
1491:
1454:
1450:
1440:
1405:
1401:
1391:
1366:
1362:
1356:
1323:
1319:
1313:
1276:
1272:
1234:
1230:
1224:
1197:
1193:
1187:
1151:
1148:Biochemistry
1147:
1143:
1107:
1103:
1093:
1058:
1054:
1044:
1019:
1015:
1003:
960:
956:
904:
900:
888:
855:
851:
803:
797:
776:cite journal
699:
692:
677:Huntington's
674:
654:
643:
639:kynureninase
592:
520:
466:
451:
436:
408:
347:through the
335:
331:
327:
318:
308:
236:
230:
92:BRENDA entry
2527:Active site
1451:J. Neurosci
681:Alzheimer's
433:Active site
427:hydrophobic
292:-kynurenine
267:-kynurenine
80:IntEnz view
40:Identifiers
2805:EC 1.14.13
2799:Categories
2730:Isomerases
2704:Hydrolases
2571:Regulation
2412:Tyrosinase
2379:: reduced
2342:: reduced
2310:: reduced
2274:: reduced
1935:Proteomics
1751:(12): 12.
1555:Curr. Biol
1549:Drosophila
1502:Nat. Genet
1016:J. Biochem
744:References
722:kynurenine
710:kynurenine
694:Drosophila
689:huntingtin
665:antagonist
663:and as an
657:antagonist
623:3-hydroxy-
621:neurotoxin
611:tryptophan
311:KMO (gene)
286:3-hydroxy-
233:enzymology
149:structures
116:KEGG entry
63:9029-61-2
2609:EC number
2381:ascorbate
2344:pteridine
872:1359-6446
706:cytokines
517:Mechanism
405:Structure
252:catalyzes
244:1.14.13.9
69:Databases
51:1.14.13.9
2633:Kinetics
2557:Cofactor
2520:Activity
2039:13502353
1963:24074942
1955:16526094
1879:24836604
1839:PLOS ONE
1820:39150343
1812:17665285
1777:24567701
1726:21693093
1677:21727251
1620:20658274
1585:21636279
1532:15806102
1483:11567036
1432:22678511
1348:28669340
1305:24189070
1251:20942784
1168:18954092
1126:10672018
1085:26752518
1036:20802227
995:23575632
880:26589832
830:38080353
555:ketimine
541:. After
415:subunits
398:homology
370:cofactor
246:) is an
220:proteins
208:articles
196:articles
153:RCSB PDB
2789:Biology
2743:Ligases
2513:Enzymes
2427:1.14.99
2405:: other
2399:1.14.18
2377:1.14.17
2340:1.14.16
2308:1.14.15
2272:1.14.14
2172:1.14.13
2099:1.14.11
1992:6076241
1920:4168935
1870:4023975
1847:Bibcode
1768:3915289
1717:3244499
1668:3855543
1628:3225744
1576:3929356
1523:1449881
1474:6762893
1423:3681811
1383:6268428
1340:1686636
1296:3868768
1076:4871268
986:3736096
965:Bibcode
921:5087636
659:of the
509:and Tyr
423:α-helix
419:β-sheet
175:QuickGO
140:profile
123:MetaCyc
58:CAS no.
2775:Portal
2717:Lyases
2276:flavin
2155:ALKBH1
2037:
1990:
1961:
1953:
1918:
1877:
1867:
1818:
1810:
1775:
1765:
1724:
1714:
1675:
1665:
1626:
1618:
1583:
1573:
1530:
1520:
1481:
1471:
1430:
1420:
1381:
1346:
1338:
1303:
1293:
1249:
1216:816794
1214:
1166:
1124:
1083:
1073:
1034:
993:
983:
957:Nature
919:
878:
870:
828:
818:
683:, and
384:, and
334:, and
313:. The
248:enzyme
203:PubMed
185:Search
171:AmiGO
159:PDBsum
99:ExPASy
87:BRENDA
75:IntEnz
46:EC no.
16:Enzyme
2669:Types
2445:HMOX1
2180:NADPH
2138:P4HTM
2131:EGLN3
2126:EGLN2
2121:EGLN1
2092:1.14)
1959:S2CID
1816:S2CID
1624:S2CID
1344:S2CID
826:S2CID
491:, Phe
487:, Pro
483:, Phe
479:, Leu
475:, Ile
471:, Met
454:-face
411:dimer
394:yeast
271:NADPH
250:that
135:PRIAM
2761:list
2754:EC7
2748:list
2741:EC6
2735:list
2728:EC5
2722:list
2715:EC4
2709:list
2702:EC3
2696:list
2689:EC2
2683:list
2676:EC1
2461:21A2
2456:17A1
2330:11A1
2325:11B2
2320:11B1
2288:19A1
2235:NOS3
2230:NOS2
2225:NOS1
2213:FMO5
2208:FMO4
2203:FMO3
2198:FMO2
2193:FMO1
2176:NADH
2150:AlkB
2035:PMID
1988:PMID
1951:PMID
1916:PMID
1875:PMID
1808:PMID
1773:PMID
1722:PMID
1673:PMID
1616:PMID
1581:PMID
1528:PMID
1479:PMID
1428:PMID
1379:PMID
1336:PMID
1301:PMID
1247:PMID
1212:PMID
1164:PMID
1122:PMID
1081:PMID
1032:PMID
991:PMID
917:PMID
876:PMID
868:ISSN
816:ISBN
789:help
728:and
650:NMDA
460:–Gln
296:NADP
254:the
235:, a
215:NCBI
156:PDBe
111:KEGG
2298:2E1
2293:2D6
2278:or
2252:3A4
2178:or
2160:FTO
2025:doi
2021:229
1980:doi
1943:doi
1908:doi
1904:144
1865:PMC
1855:doi
1800:doi
1763:PMC
1753:doi
1712:PMC
1704:doi
1663:PMC
1655:doi
1608:doi
1571:PMC
1563:doi
1518:PMC
1510:doi
1469:PMC
1459:doi
1418:PMC
1410:doi
1371:doi
1328:doi
1291:PMC
1281:doi
1277:288
1239:doi
1202:doi
1198:251
1156:doi
1112:doi
1108:267
1071:PMC
1063:doi
1024:doi
1020:148
981:PMC
973:doi
961:496
909:doi
905:352
860:doi
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