488:-specific). Other names in common use include pyridine nucleotide transhydrogenase, transhydrogenase, NAD(P)+ transhydrogenase, nicotinamide adenine dinucleotide (phosphate) transhydrogenase, NAD+ transhydrogenase, NADH transhydrogenase, nicotinamide nucleotide transhydrogenase, NADPH-NAD+ transhydrogenase, pyridine nucleotide transferase, NADPH-NAD+ oxidoreductase, NADH-NADP+-transhydrogenase, NADPH:NAD+ transhydrogenase, H+-Thase, energy-linked transhydrogenase, and NAD(P)+ transhydrogenase (AB-specific).
1138:
1118:
29:
574:
427:
132:
335:
88:
76:
354:
612:
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567:
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673:
837:
608:
587:
454:
442:
1206:
785:
664:
347:
1211:
504:
Fisher RR, Earle SR (1982). "Membrane-Bournd
Pyridine Dinucleotide Transhydrogenases". In Everse J, Anderson B, You K (eds.).
274:
993:
298:
152:
1221:
1175:
720:
715:
710:
804:
523:
You KS (1985). "Stereospecificity for nicotinamide nucleotides in enzymatic and chemical hydride transfer reactions".
1108:
978:
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1081:
1068:
1055:
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1029:
1016:
795:
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749:
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604:
988:
1168:
942:
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595:
434:
388:
292:
185:
140:
890:
678:
659:
279:
464:, specifically those acting on NADH or NADPH with NAD+ or NADP+ as acceptor. This enzyme participates in
412:
911:
830:
359:
983:
267:
136:
1137:
202:
947:
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295:
880:
762:
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926:
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119:
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147:
1050:
705:
651:
250:
109:
64:
52:
819:
556:
28:
33:
NAD(P) transhydrogenase heterotrimer, Rhodospirillum rubrum
815:
416:
1156:
1106:
415:
1002:
966:
935:
904:
853:
794:
771:
748:
687:
646:
603:
480:
of this enzyme class is NADPH:NAD+ oxidoreductase (
353:
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329:
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285:
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261:
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508:. Burlington: Elsevier Science. pp. 279–324.
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831:
568:
8:
1183:
1169:
838:
824:
816:
575:
561:
553:
321:
100:
414:
1113:
466:nicotinate and nicotinamide metabolism
163:
18:
460:This enzyme belongs to the family of
7:
1134:
1132:
525:CRC Critical Reviews in Biochemistry
422:{\displaystyle \rightleftharpoons }
14:
506:The Pyridine Nucleotide Coenzymes
1136:
1116:
786:Trimethylamine-N-oxide reductase
27:
1:
721:Neutrophil cytosolic factor 4
716:Neutrophil cytosolic factor 2
711:Neutrophil cytosolic factor 1
674:NADPH—cytochrome-c2 reductase
104:Available protein structures:
1155:. You can help Knowledge by
805:NADH dehydrogenase (quinone)
665:NADPH—hemoprotein reductase
1238:
1217:Enzymes of known structure
1131:
994:Michaelis–Menten kinetics
669:Cytochrome P450 reductase
630:NAD(P) transhydrogenase (
621:NAD(P) transhydrogenase (
537:10.3109/10409238509113625
377:NAD(P) transhydrogenase (
320:
167:NAD(P) transhydrogenase (
99:
26:
886:Diffusion-limited enzyme
1207:NADPH-dependent enzymes
679:Leghemoglobin reductase
660:Methemoglobin reductase
22:NAD(P) transhydrogenase
1212:NADH-dependent enzymes
1151:-related article is a
423:
979:Eadie–Hofstee diagram
912:Allosteric regulation
424:
1222:Oxidoreductase stubs
989:Lineweaver–Burk plot
413:
437:of this enzyme are
948:Enzyme superfamily
881:Enzyme promiscuity
763:NADH dehydrogenase
445:, whereas its two
419:
1164:
1163:
1104:
1103:
813:
812:
515:978-0-323-15084-2
404:chemical reaction
369:
368:
365:
364:
268:metabolic pathway
162:
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158:
157:
153:structure summary
1229:
1185:
1178:
1171:
1140:
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1121:
1120:
1112:
984:Hanes–Woolf plot
927:Enzyme activator
922:Enzyme inhibitor
896:Enzyme catalysis
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1105:
1100:
1012:Oxidoreductases
998:
974:Enzyme kinetics
962:
958:List of enzymes
931:
900:
871:Catalytic triad
849:
844:
814:
809:
790:
767:
744:
683:
642:
599:
584:Oxidoreductases
581:
551:
522:
516:
503:
499:
497:Further reading
494:
478:systematic name
474:
462:oxidoreductases
411:
410:
77:OPM superfamily
34:
17:
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11:
5:
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936:Classification
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769:
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757:
746:
745:
743:
742:
741:
740:
738:Dual oxidase 2
735:
733:Dual oxidase 1
725:
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713:
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531:(4): 313–451.
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433:Thus, the two
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987:
985:
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977:
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954:
953:Enzyme family
951:
949:
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938:
934:
928:
925:
923:
920:
918:
917:Cooperativity
915:
913:
910:
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903:
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894:
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876:Oxyanion hole
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852:
848:
841:
836:
834:
829:
827:
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821:
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803:
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797:
793:
787:
784:
783:
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764:
761:
760:
758:
755:
751:
747:
739:
736:
734:
731:
730:
729:
726:
722:
719:
717:
714:
712:
709:
707:
704:
703:
702:
701:NADPH oxidase
699:
698:
696:
694:
690:
686:
680:
677:
675:
672:
670:
666:
663:
661:
658:
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571:
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559:
558:
555:
546:
542:
538:
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530:
526:
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517:
511:
507:
502:
501:
496:
491:
489:
487:
483:
479:
471:
469:
467:
463:
458:
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448:
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436:
408:
407:
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405:
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397:
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352:
349:
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340:
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328:
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316:
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309:
307:
306:Gene Ontology
303:
300:
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288:
284:
281:
278:
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266:
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260:
257:
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244:NiceZyme view
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59:
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54:
50:
46:
42:
37:
30:
25:
20:
1157:expanding it
1143:
1128:
1090:Translocases
1087:
1074:
1061:
1048:
1035:
1025:Transferases
1022:
1009:
866:Binding site
728:dual oxidase
727:
635:
631:
629:
622:
528:
524:
505:
485:
481:
475:
472:Nomenclature
459:
432:
409:NADPH + NAD
382:
378:
376:
370:
232:BRENDA entry
172:
168:
16:Enzyme class
861:Active site
777:Nitrogenous
429:NADP + NADH
220:IntEnz view
180:Identifiers
89:OPM protein
39:Identifiers
1196:Categories
1064:Isomerases
1038:Hydrolases
905:Regulation
756:or similar
638:-specific)
625:-specific)
492:References
435:substrates
373:enzymology
289:structures
256:KEGG entry
203:9014-18-0
116:structures
943:EC number
417:⇌
400:catalyzes
385:-specific
209:Databases
175:-specific
1202:EC 1.6.1
967:Kinetics
891:Cofactor
854:Activity
706:P91-PHOX
447:products
394:) is an
360:proteins
348:articles
336:articles
293:RCSB PDB
133:RCSB PDB
1123:Biology
1077:Ligases
847:Enzymes
798:: other
754:Quinone
545:3157549
392:1.6.1.2
315:QuickGO
280:profile
263:MetaCyc
198:CAS no.
191:1.6.1.2
58:PF02233
1149:enzyme
1146:EC 1.6
1109:Portal
1051:Lyases
796:1.6.99
693:Oxygen
543:
512:
396:enzyme
343:PubMed
325:Search
311:AmiGO
299:PDBsum
239:ExPASy
227:BRENDA
215:IntEnz
186:EC no.
148:PDBsum
122:
112:
44:Symbol
1144:This
1003:Types
779:group
773:1.6.6
750:1.6.5
689:1.6.3
648:1.6.2
605:1.6.1
592:NADPH
439:NADPH
398:that
275:PRIAM
70:3.D.2
1153:stub
1095:list
1088:EC7
1082:list
1075:EC6
1069:list
1062:EC5
1056:list
1049:EC4
1043:list
1036:EC3
1030:list
1023:EC2
1017:list
1010:EC1
652:Heme
613:NADP
598:1.6)
588:NADH
541:PMID
510:ISBN
476:The
455:NADH
453:and
451:NADP
449:are
441:and
402:the
375:, a
355:NCBI
296:PDBe
251:KEGG
141:PDBj
137:PDBe
120:ECOD
110:Pfam
94:4o9u
65:TCDB
53:Pfam
609:NAD
590:or
533:doi
443:NAD
371:In
331:PMC
287:PDB
128:PDB
82:410
1198::
775::
752::
691::
650::
636:Si
632:Re
623:Si
607::
596:EC
586::
539:.
529:17
527:.
486:Si
482:Re
468:.
457:.
389:EC
383:Si
379:Re
313:/
173:Si
169:Re
139:;
135:;
118:/
1184:e
1177:t
1170:v
1159:.
1111::
1097:)
1093:(
1084:)
1080:(
1071:)
1067:(
1058:)
1054:(
1045:)
1041:(
1032:)
1028:(
1019:)
1015:(
839:e
832:t
825:v
667:/
634:/
611:/
594:(
576:e
569:t
562:v
547:.
535::
518:.
484:/
387:(
381:/
171:/
47:?
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