29:
853:
Jensen, Simon Bo; Thodberg, Sara; Parween, Shaheena; Moses, Matias E.; Hansen, Cecilie C.; Thomsen, Johannes; Sletfjerding, Magnus B.; Knudsen, Camilla; Del
Giudice, Rita; Lund, Philip M.; Castaño, Patricia R. (2021-04-15).
970:
Daniel, R.A.; Errington, J. (1993). "Cloning, DNA Sequence, Functional
Analysis and Transcriptional Regulation of the Genes Encoding Dipicolinic Acid Synthetase Required for Sporulation in Bacillus subtilis".
206:, wherein the FAD is buried deeply). About 5-10% of flavoproteins have a covalently linked FAD. Based on the available structural data, FAD-binding sites can be divided into more than 200 different types.
1006:
Clausen, Monika; Lamb, Christopher J.; Megnet, Roland; Doerner, Peter W. (1994). "PAD1 encodes phenylacrylic acid decarboxylase which confers resistance to cinnamic acid in
Saccharomyces cerevisiae".
290:, but mixing of the two restored the enzyme activity. However, replacing the isolated pigment with riboflavin did not restore enzyme activity, despite being indistinguishable under
543:
Garma, Leonardo D.; Medina, Milagros; Juffer, André H. (2016-11-01). "Structure-based classification of FAD binding sites: A comparative study of structural alignment tools".
209:
90 flavoproteins are encoded in the human genome; about 84% require FAD and around 16% require FMN, whereas 5 proteins require both. Flavoproteins are mainly located in the
388:
128:
374:
1102:
provides A comprehensive collection of all flavo-proteins with known 3D-structure. It compares the protein structures to elucidate phylogenetic relationships.
488:"Genetic Control of Biosynthesis and Transport of Riboflavin and Flavin Nucleotides and Construction of Robust Biotechnological Producers"
338:
435:
Hanukoglu I (2017). "Conservation of the Enzyme-Coenzyme
Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous Enzyme".
1127:
327:
that is involved in steroid hormone synthesis in vertebrate species, and has a ubiquitous distribution in metazoa and prokaryotes
76:
783:
Christie, S. M. H.; Kenner, G. W.; Todd, A. R. (1954). "Nucleotides. Part XXV. A synthesis of flavin?adenine dinucleotide".
148:
1201:
245:. By the early 1930s, this same pigment had been isolated from a range of sources, and recognised as a component of the
923:"Purification and characterization of EpiD, a flavoprotein involved in the biosynthesis of the lantibiotic epidermin"
1186:
136:
807:
1120:
309:
195:
132:
1261:
1166:
1161:
330:
89:
856:"Biased cytochrome P450-mediated metabolism via small-molecule ligands binding P450 oxidoreductase"
392:
764:
Warburg, O.; Christian, W. (1938). "Isolation of the prosthetic group of the amino acid oxydase".
1196:
1181:
1176:
260:
199:
1156:
1113:
345:
1226:
1151:
707:
324:
295:
203:
191:
175:. These proteins are involved in a wide array of biological processes, including removal of
867:
444:
302:
275:
115:
8:
359:
176:
871:
745:
Theorell, H. (1935). "Preparation in pure state of the effect group of yellow enzymes".
448:
1206:
1078:
898:
855:
685:
623:
598:
576:
520:
487:
468:
253:, derived from the ribityl side chain and yellow colour of the conjugated ring system.
947:
922:
1266:
1221:
1216:
1082:
1070:
1062:
1023:
1019:
988:
952:
938:
903:
885:
835:
827:
823:
727:
677:
669:
664:
647:
628:
568:
560:
525:
507:
460:
282:
and a bright-yellow pigment. Neither apoprotein nor pigment alone could catalyse the
246:
123:
81:
1043:"Flavoprotein Photochemistry: Fundamental Processes and Photocatalytic Perspectives"
1042:
689:
580:
333:
that is a redox partner of cytochrome P450 proteins located in endoplasmic reticulum
57:
1054:
1015:
980:
942:
934:
893:
875:
819:
788:
719:
659:
618:
610:
552:
515:
499:
472:
452:
382:
111:
237:
Flavoproteins were first mentioned in 1879, when they isolated as a bright-yellow
1247:
294:. This led to the discovery that the protein studied required not riboflavin but
69:
723:
880:
180:
614:
456:
1255:
1211:
1066:
1058:
889:
831:
673:
564:
511:
399:
264:
648:"Flavogenomics – a genomic and structural view of flavin-dependent proteins"
1171:
1074:
984:
907:
839:
808:"NADPH P450 oxidoreductase: Structure, function, and pathology of diseases"
731:
681:
632:
597:
Lienhart, Wolf-Dieter; Gudipati, Venugopal; Macheroux, Peter (2013-07-15).
572:
529:
464:
412:
341:
291:
214:
210:
168:
1027:
992:
956:
503:
213:. Of all flavoproteins, 90% perform redox reactions and the other 10% are
85:
1105:
792:
408:
395:
367:
320:
The flavoprotein family contains a diverse range of enzymes, including:
1191:
556:
250:
249:. Its structure was determined and reported in 1935 and given the name
222:
184:
172:
187:. The flavoproteins are some of the most-studied families of enzymes.
378:
352:
283:
279:
1243:
646:
Macheroux, Peter; Kappes, Barbara; Ealick, Steven E. (2011-08-01).
356:
164:
64:
1136:
271:
238:
226:
349:
257:
218:
143:
28:
344:
protein, EpiD, which has been shown to be a flavoprotein that
403:
268:
1239:
287:
105:
52:
1099:
852:
596:
1041:
Zhuang, Bo; Liebl, Ursula; Vos, Marten H. (2022-05-05).
1005:
920:
708:"The chemical and biological versatility of riboflavin"
256:
The first evidence for the requirement of flavin as an
1238:
This article incorporates text from the public domain
921:
Kupke, T; Stevanović, S; Sahl, H. G.; Götz, F (1992).
312:(FAD) as a second form of flavin utilised by enzymes.
645:
486:
Abbas, Charles A.; Sibirny, Andriy A. (2011-06-01).
430:
428:
267:and coworkers showed that a bright-yellow-coloured
782:
806:Pandey, Amit V.; FlĂĽck, Christa E. (2013-05-01).
545:Proteins: Structure, Function, and Bioinformatics
542:
425:
355:the removal of two reducing equivalents from the
1253:
763:
969:
202:. The flavin is generally tightly bound (as in
1040:
1121:
485:
241:from cow's milk. They were initially termed
999:
963:
914:
805:
370:of epidermin to form a --C==C-- double bond
1135:
1128:
1114:
492:Microbiology and Molecular Biology Reviews
27:
946:
897:
879:
663:
622:
519:
434:
398:), an enzyme which confers resistance to
274:, identified previously as essential for
744:
701:
699:
603:Archives of Biochemistry and Biophysics
1254:
705:
1109:
696:
592:
590:
1202:Methylenetetrahydrofolate reductase
1047:The Journal of Physical Chemistry B
13:
1098:The menu "science" of the program
179:contributing to oxidative stress,
14:
1278:
1092:
587:
939:10.1128/jb.174.16.5354-5361.1992
824:10.1016/j.pharmthera.2013.01.010
712:Biochemical Society Transactions
665:10.1111/j.1742-4658.2011.08202.x
389:Phenylacrylic acid decarboxylase
198:) as a prosthetic group or as a
1034:
846:
812:Pharmacology & Therapeutics
799:
785:Journal of the Chemical Society
190:Flavoproteins have either FMN (
1187:Dihydrolipoamide dehydrogenase
776:
757:
738:
639:
536:
479:
437:Journal of Molecular Evolution
385:from dihydroxydipicolinic acid
33:the fmn binding protein athal3
1:
419:
308:led to the identification of
100:Available protein structures:
1020:10.1016/0378-1119(94)90363-8
973:Journal of Molecular Biology
298:to be catalytically active.
232:
7:
315:
310:flavin adenine dinucleotide
196:flavin adenine dinucleotide
10:
1283:
1237:
881:10.1038/s41467-021-22562-w
278:, could be separated into
1167:Butyryl CoA dehydrogenase
1162:Apoptosis-inducing factor
1147:
724:10.1042/0300-5127:0280283
615:10.1016/j.abb.2013.02.015
599:"The human flavoproteome"
457:10.1007/s00239-017-9821-9
331:Cytochrome P450 reductase
301:Similar experiments with
142:
122:
104:
99:
95:
75:
63:
51:
43:
38:
26:
21:
1059:10.1021/acs.jpcb.2c00969
766:Biochemische Zeitschrift
747:Biochemische Zeitschrift
415:, light-sensing proteins
1197:Methemoglobin reductase
1182:Cytokinin dehydrogenase
1177:Cytochrome b5 reductase
927:Journal of Bacteriology
1157:Acyl CoA dehydrogenase
985:10.1006/jmbi.1993.1403
1227:Thioredoxin reductase
1152:Acetolactate synthase
860:Nature Communications
504:10.1128/MMBR.00030-10
375:dipicolinate synthase
325:Adrenodoxin reductase
296:flavin mononucleotide
204:adrenodoxin reductase
192:flavin mononucleotide
793:10.1039/JR9540000046
276:cellular respiration
872:2021NatCo..12.2260J
449:2017JMolE..85..205H
306:-amino acid oxidase
1207:NADH dehydrogenase
706:Massey, V (2000).
557:10.1002/prot.25158
377:, an enzyme which
362:of the C-terminal
1235:
1234:
1222:Sarcosine oxidase
1217:Nitrate reductase
1053:(17): 3199–3207.
658:(15): 2625–2634.
551:(11): 1728–1747.
381:the formation of
305:
247:vitamin B complex
158:
157:
154:
153:
149:structure summary
1274:
1262:Protein families
1130:
1123:
1116:
1107:
1106:
1087:
1086:
1038:
1032:
1031:
1003:
997:
996:
967:
961:
960:
950:
918:
912:
911:
901:
883:
850:
844:
843:
803:
797:
796:
780:
774:
773:
761:
755:
754:
742:
736:
735:
703:
694:
693:
667:
643:
637:
636:
626:
594:
585:
584:
540:
534:
533:
523:
483:
477:
476:
432:
383:dipicolinic acid
303:
97:
96:
31:
19:
18:
1282:
1281:
1277:
1276:
1275:
1273:
1272:
1271:
1252:
1251:
1250:
1236:
1231:
1143:
1134:
1095:
1090:
1039:
1035:
1004:
1000:
968:
964:
933:(16): 5354–61.
919:
915:
851:
847:
804:
800:
781:
777:
762:
758:
743:
739:
704:
697:
644:
640:
595:
588:
541:
537:
484:
480:
433:
426:
422:
373:The B chain of
318:
235:
167:that contain a
34:
17:
12:
11:
5:
1280:
1270:
1269:
1264:
1233:
1232:
1230:
1229:
1224:
1219:
1214:
1209:
1204:
1199:
1194:
1189:
1184:
1179:
1174:
1169:
1164:
1159:
1154:
1148:
1145:
1144:
1133:
1132:
1125:
1118:
1110:
1104:
1103:
1094:
1093:External links
1091:
1089:
1088:
1033:
998:
962:
913:
845:
818:(2): 229–254.
798:
775:
756:
737:
695:
638:
609:(2): 150–162.
586:
535:
498:(2): 321–360.
478:
443:(5): 205–218.
423:
421:
418:
417:
416:
406:
386:
371:
335:
334:
328:
317:
314:
263:came in 1935.
234:
231:
181:photosynthesis
171:derivative of
156:
155:
152:
151:
146:
140:
139:
126:
120:
119:
109:
102:
101:
93:
92:
79:
73:
72:
67:
61:
60:
55:
49:
48:
45:
41:
40:
36:
35:
32:
24:
23:
16:Protein family
15:
9:
6:
4:
3:
2:
1279:
1268:
1265:
1263:
1260:
1259:
1257:
1249:
1245:
1241:
1228:
1225:
1223:
1220:
1218:
1215:
1213:
1212:NADPH oxidase
1210:
1208:
1205:
1203:
1200:
1198:
1195:
1193:
1190:
1188:
1185:
1183:
1180:
1178:
1175:
1173:
1170:
1168:
1165:
1163:
1160:
1158:
1155:
1153:
1150:
1149:
1146:
1142:
1141:flavoproteins
1138:
1131:
1126:
1124:
1119:
1117:
1112:
1111:
1108:
1101:
1097:
1096:
1084:
1080:
1076:
1072:
1068:
1064:
1060:
1056:
1052:
1048:
1044:
1037:
1029:
1025:
1021:
1017:
1014:(1): 107–12.
1013:
1009:
1002:
994:
990:
986:
982:
979:(2): 468–83.
978:
974:
966:
958:
954:
949:
944:
940:
936:
932:
928:
924:
917:
909:
905:
900:
895:
891:
887:
882:
877:
873:
869:
865:
861:
857:
849:
841:
837:
833:
829:
825:
821:
817:
813:
809:
802:
794:
790:
786:
779:
771:
767:
760:
752:
748:
741:
733:
729:
725:
721:
718:(4): 283–96.
717:
713:
709:
702:
700:
691:
687:
683:
679:
675:
671:
666:
661:
657:
653:
649:
642:
634:
630:
625:
620:
616:
612:
608:
604:
600:
593:
591:
582:
578:
574:
570:
566:
562:
558:
554:
550:
546:
539:
531:
527:
522:
517:
513:
509:
505:
501:
497:
493:
489:
482:
474:
470:
466:
462:
458:
454:
450:
446:
442:
438:
431:
429:
424:
414:
410:
407:
405:
401:
400:cinnamic acid
397:
394:
390:
387:
384:
380:
376:
372:
369:
365:
361:
358:
354:
351:
347:
343:
340:
337:
336:
332:
329:
326:
323:
322:
321:
313:
311:
307:
299:
297:
293:
289:
285:
281:
277:
273:
270:
266:
265:Hugo Theorell
262:
259:
254:
252:
248:
244:
240:
230:
228:
224:
220:
216:
212:
207:
205:
201:
197:
193:
188:
186:
182:
178:
174:
170:
166:
162:
161:Flavoproteins
150:
147:
145:
141:
138:
134:
130:
127:
125:
121:
117:
113:
110:
107:
103:
98:
94:
91:
87:
83:
80:
78:
74:
71:
68:
66:
62:
59:
56:
54:
50:
46:
42:
37:
30:
25:
20:
1172:Cryptochrome
1140:
1050:
1046:
1036:
1011:
1007:
1001:
976:
972:
965:
930:
926:
916:
863:
859:
848:
815:
811:
801:
784:
778:
769:
765:
759:
750:
746:
740:
715:
711:
655:
652:FEBS Journal
651:
641:
606:
602:
548:
544:
538:
495:
491:
481:
440:
436:
413:cryptochrome
363:
342:biosynthesis
319:
300:
292:spectroscopy
255:
242:
236:
215:transferases
211:mitochondria
208:
189:
169:nucleic acid
160:
159:
47:Flavoprotein
22:Flavoprotein
866:(1): 2260.
409:Phototropin
368:lanthionine
243:lactochrome
39:Identifiers
1256:Categories
1192:Flavodoxin
420:References
348:FMN. This
280:apoprotein
251:riboflavin
223:isomerases
194:) or FAD (
185:DNA repair
173:riboflavin
112:structures
1248:IPR003382
1083:248296520
1067:1520-6106
890:2041-1723
832:0163-7258
787:: 46–52.
772:: 150–68.
753:: 344–46.
674:1742-4658
565:1097-0134
512:1092-2172
396:4.1.1.102
379:catalyses
353:catalyses
339:Epidermin
284:oxidation
233:Discovery
70:IPR003382
1267:Proteins
1244:InterPro
1075:35442696
908:33859207
840:23353702
732:10961912
690:22220250
682:21635694
633:23500531
581:26066208
573:27580869
530:21646432
465:29177972
357:cysteine
316:Examples
261:cofactor
200:cofactor
177:radicals
165:proteins
129:RCSB PDB
65:InterPro
1137:Protein
1028:8181743
993:8345520
957:1644762
899:8050233
868:Bibcode
624:3684772
521:3122625
473:7120148
445:Bibcode
360:residue
272:protein
239:pigment
227:ligases
58:PF02441
1081:
1073:
1065:
1026:
991:
955:
948:206373
945:
906:
896:
888:
838:
830:
730:
688:
680:
672:
631:
621:
579:
571:
563:
528:
518:
510:
471:
463:
350:enzyme
258:enzyme
219:lyases
183:, and
144:PDBsum
118:
108:
90:SUPFAM
44:Symbol
1100:STRAP
1079:S2CID
686:S2CID
577:S2CID
469:S2CID
404:yeast
346:binds
269:yeast
86:SCOPe
77:SCOP2
1242:and
1240:Pfam
1071:PMID
1063:ISSN
1024:PMID
1008:Gene
989:PMID
953:PMID
904:PMID
886:ISSN
836:PMID
828:ISSN
728:PMID
678:PMID
670:ISSN
629:PMID
569:PMID
561:ISSN
526:PMID
508:ISSN
461:PMID
411:and
364:meso
288:NADH
163:are
137:PDBj
133:PDBe
116:ECOD
106:Pfam
82:1e20
53:Pfam
1055:doi
1051:126
1016:doi
1012:142
981:doi
977:232
943:PMC
935:doi
931:174
894:PMC
876:doi
820:doi
816:138
789:doi
770:298
751:275
720:doi
660:doi
656:278
619:PMC
611:doi
607:535
553:doi
516:PMC
500:doi
453:doi
402:in
286:of
124:PDB
1258::
1246::
1139::
1077:.
1069:.
1061:.
1049:.
1045:.
1022:.
1010:.
987:.
975:.
951:.
941:.
929:.
925:.
902:.
892:.
884:.
874:.
864:12
862:.
858:.
834:.
826:.
814:.
810:.
768:.
749:.
726:.
716:28
714:.
710:.
698:^
684:.
676:.
668:.
654:.
650:.
627:.
617:.
605:.
601:.
589:^
575:.
567:.
559:.
549:84
547:.
524:.
514:.
506:.
496:75
494:.
490:.
467:.
459:.
451:.
441:85
439:.
427:^
393:EC
229:.
225:,
221:,
217:,
135:;
131:;
114:/
88:/
84:/
1129:e
1122:t
1115:v
1085:.
1057::
1030:.
1018::
995:.
983::
959:.
937::
910:.
878::
870::
842:.
822::
795:.
791::
734:.
722::
692:.
662::
635:.
613::
583:.
555::
532:.
502::
475:.
455::
447::
391:(
366:-
304:D
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.
