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1.14.13.39: nitric-oxide synthase (NADPH)

This is an abbreviated version!
For detailed information about nitric-oxide synthase (NADPH), go to the full flat file.

Word Map on EC 1.14.13.39

Reaction

2 L-arginine + 2 NADPH + 2 H+ + 2 O2 = 2 Nomega-hydroxy-L-arginine + 2 NADP+ + 2 H2O

Synonyms

bacterial nitric oxide synthase, bacterial nitric-oxide synthase, bNOS, bsNOS, cb-NOS, cytokine inducible NOS, DNOS, e-NOS, EC-NOS, endothelial nitric oxide synthase, endothelial nitric-oxide synthase, endothelial NO synthase, endothelial NOS, endothelium-derived relaxation factor-forming enzyme, endothelium-derived relaxing factor synthase, eNOS, i-NOS, inducible nitric oxide synthase, inducible nitric-oxide synthase, inducible NO synthase, inducible NOS, iNOS, mitochondrial NO synthase, mitochondrial-specific nitric oxide synthase, mtNOS, n-NOS, NADPH diaphorase, NADPH-d, NADPH-diaphorase, NADPHd, neuronal nitric oxide synthase, neuronal nitric-oxide synthase, neuronal NO synthase, neuronal NOS, nicotinamide adenine dinucleotide phosphate-diaphorase, nitric oxid synthase, nitric oxide synthase, nitric oxide synthase-like protein, nitric oxide synthetase, nitric-oxide synthase, nNOS, nNOSalpha, NO synthase, NO synthase type I, NO synthase type II, NO synthase type III, NO-synthase, NOS, NOS I, NOS-2, NOS1, NOS2, NOS3, synthetase, nitric oxide

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.13.39 nitric-oxide synthase (NADPH)

pH Stability

pH Stability on EC 1.14.13.39 - nitric-oxide synthase (NADPH)

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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
subunit disassembly and unfolding of the protein following a pH jump from 7.5 to 2.8, kinetic unfolding mechanism of the inducible enzymes' oxygenase domain, the initial step of the reaction is the disruption of the iNOSCOD dimer, to generate heme-bound monomeric species in various degrees of unfolding, which is accompanied by the loss of two tetrahydrobiopterin cofactors, subsequent heme loss generates monomeric apoproteins exhibiting various degrees of unfolding, modeling of the denaturation process, overview
672016