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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)

Posttranslational Modification

Posttranslational Modification on EC 1.14.13.39 - nitric-oxide synthase (NADPH)

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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
flavoprotein
glycoprotein
lipoprotein
in PE placentas, eNOS can be posttranslationally modified by lipid peroxidation-derived aldehydes such as malondialdehyde or as 4-oxononenal (ONE) a highly bioreactive agent, able to inhibit eNOS activity and NO production. They covalently bind to the nucleophilic sulfhydryl and primary amine groups of proteins, forming Schiff bases, Michael adducts and protein crosslinks. The modification of proteins by lipid peroxidation products (LPPs) depends on their nature, expression and conformation, oxidative stress intensity and duration, cell type, local LPP concentration, and generates various biological responses from the expression of protective and adaptive factors to protein dysfunction, inflammation, senescence and apoptosis. The presence of LPPs in PE placentas, could be indicative of their premature senescence, in agreement with the hypothesis that accelerated placental aging is involved in PE pathophysiology via oxidative stress
sumoylation
isoform neuronal nitric oxide synthase is clearly a SUMO-1 target protein both in vitro and at the cellular level. SUMO-1 conjugation of neuronal nitric oxide synthase depends on Ubc9 (E2). The interaction between neuronal nitric oxide synthase and Ubc9 is facilitated by PIASxbeta (E3) and SUMO-1 is deconjugated from neuronal nitric oxide synthase by SENP1 and SENP2
additional information