ID   1.14.13.39
DE   nitric-oxide synthase (NADPH).
AN   endothelium-derived relaxation factor-forming enzyme.
AN   endothelium-derived relaxing factor synthase.
AN   NADPH-diaphorase.
AN   nitric-oxide synthetase.
AN   NO synthase.
CA   H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline + 3 NADP(+)
CA   + 2 nitric oxide.
CC   -!- The enzyme consists of linked oxygenase and reductase domains.
CC   -!- The eukaryotic enzyme binds FAD, FMN, heme (iron protoporphyrin IX)
CC       and tetrahydrobiopterin, and its two domains are linked via a
CC       regulatory calmodulin-binding domain.
CC   -!- Upon calcium-induced calmodulin binding, the reductase and oxygenase
CC       domains form a complex, allowing electrons to flow from NADPH via FAD
CC       and FMN to the active center.
CC   -!- The reductase domain of the enzyme from the bacterium Sorangium
CC       cellulosum utilizes a [2Fe-2S] cluster to transfer the electrons from
CC       NADPH to the active center. cf. EC 1.14.14.47.
DR   Q66GP9, NOA1_ARATH ;  P29475, NOS1_HUMAN ;  Q9Z0J4, NOS1_MOUSE ;
DR   O19132, NOS1_RABIT ;  P29476, NOS1_RAT   ;  Q29498, NOS1_SHEEP ;
DR   Q27995, NOS2_BOVIN ;  O62699, NOS2_CANLF ;  Q28314, NOS2_CAPHI ;
DR   Q92037, NOS2_CARAU ;  O54705, NOS2_CAVPO ;  Q90703, NOS2_CHICK ;
DR   P35228, NOS2_HUMAN ;  O46660, NOS2_MACMU ;  P29477, NOS2_MOUSE ;
DR   Q92091, NOS2_ONCMY ;  P79290, NOS2_PIG   ;  O19114, NOS2_RABIT ;
DR   Q06518, NOS2_RAT   ;  P29473, NOS3_BOVIN ;  Q9TUX8, NOS3_CANLF ;
DR   P97270, NOS3_CAVPO ;  P29474, NOS3_HUMAN ;  P70313, NOS3_MOUSE ;
DR   Q28969, NOS3_PIG   ;  Q62600, NOS3_RAT   ;  P79209, NOS3_SHEEP ;
DR   B1B557, NOSL_BOMMO ;  O61608, NOS_ANOST  ;  Q8T8C0, NOS_BOMMO  ;
DR   Q27571, NOS_DROME  ;  O61309, NOS_LYMST  ;  Q6YPG5, NOS_ORYSJ  ;
DR   Q26240, NOS_RHOPR  ;  Q9I9M2, NOS_SQUAC  ;
//