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Information on EC 1.14.13.39 - nitric-oxide synthase (NADPH) and Organism(s) Gallus gallus

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EC Tree
IUBMB Comments
The enzyme consists of linked oxygenase and reductase domains. The eukaryotic enzyme binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin, and its two domains are linked via a regulatory calmodulin-binding domain. Upon calcium-induced calmodulin binding, the reductase and oxygenase domains form a complex, allowing electrons to flow from NADPH via FAD and FMN to the active center. The reductase domain of the enzyme from the bacterium Sorangium cellulosum utilizes a [2Fe-2S] cluster to transfer the electrons from NADPH to the active center. cf. EC 1.14.14.47, nitric-oxide synthase (flavodoxin).
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Word Map
The taxonomic range for the selected organisms is: Gallus gallus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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Synonyms
nos, inducible nitric oxide synthase, endothelial nitric oxide synthase, inducible no synthase, neuronal nitric oxide synthase, inducible nos, endothelial no synthase, endothelial nos, neuronal nos, no-synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
endothelium-derived relaxation factor-forming enzyme
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endothelium-derived relaxing factor synthase
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NADPH-diaphorase
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nitric oxide synthase
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nitric oxide synthetase
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NO synthase
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synthetase, nitric oxide
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
L-arginine,NADPH:oxygen oxidoreductase (nitric-oxide-forming)
The enzyme consists of linked oxygenase and reductase domains. The eukaryotic enzyme binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin, and its two domains are linked via a regulatory calmodulin-binding domain. Upon calcium-induced calmodulin binding, the reductase and oxygenase domains form a complex, allowing electrons to flow from NADPH via FAD and FMN to the active center. The reductase domain of the enzyme from the bacterium Sorangium cellulosum utilizes a [2Fe-2S] cluster to transfer the electrons from NADPH to the active center. cf. EC 1.14.14.47, nitric-oxide synthase (flavodoxin).
CAS REGISTRY NUMBER
COMMENTARY hide
125978-95-2
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NOS2_CHICK
1136
0
129649
Swiss-Prot
other Location (Reliability: 2)
H9CZQ6_CHICK
960
0
107095
TrEMBL
Mitochondrion (Reliability: 5)
A0A1D5PXU7_CHICK
1435
0
161550
TrEMBL
other Location (Reliability: 3)
A0A1D5PZB7_CHICK
1136
0
129628
TrEMBL
other Location (Reliability: 2)
A0A3Q2UJC5_CHICK
1171
0
129937
TrEMBL
Mitochondrion (Reliability: 5)
H9CZR2_CHICK
904
0
100728
TrEMBL
other Location (Reliability: 1)
H9CZQ9_CHICK
938
0
104655
TrEMBL
other Location (Reliability: 5)
H9CZQ7_CHICK
890
0
99651
TrEMBL
Mitochondrion (Reliability: 5)
C3VQ55_CHICK
37
0
4331
TrEMBL
other Location (Reliability: 2)
H9CZR0_CHICK
882
0
98608
TrEMBL
Mitochondrion (Reliability: 5)
H9CZR1_CHICK
958
0
106803
TrEMBL
Mitochondrion (Reliability: 4)
A0A3Q2UNW2_CHICK
1402
0
153155
TrEMBL
Secretory Pathway (Reliability: 5)
H9CZQ3_CHICK
915
0
102421
TrEMBL
Mitochondrion (Reliability: 5)
H9CZP9_CHICK
985
0
109865
TrEMBL
Mitochondrion (Reliability: 5)
H9NDP8_CHICK
67
0
7866
TrEMBL
other Location (Reliability: 2)
H9CZQ0_CHICK
963
0
107425
TrEMBL
other Location (Reliability: 5)
A0A3Q2UF97_CHICK
1226
0
136044
TrEMBL
other Location (Reliability: 1)
V9ITD3_CHICK
1146
0
127459
TrEMBL
other Location (Reliability: 2)
H9CZQ1_CHICK
461
0
51863
TrEMBL
Mitochondrion (Reliability: 5)
H9CZQ5_CHICK
929
0
103317
TrEMBL
other Location (Reliability: 1)
H9CZQ8_CHICK
454
0
51109
TrEMBL
Mitochondrion (Reliability: 5)
H9CZQ4_CHICK
983
0
109573
TrEMBL
Mitochondrion (Reliability: 4)
D2XQ50_CHICK
44
0
4942
TrEMBL
Secretory Pathway (Reliability: 5)
H9CZQ2_CHICK
882
0
98589
TrEMBL
Mitochondrion (Reliability: 5)