EC Number   |
General Information |
Reference |
|---|
   1.14.13.39 | malfunction |
attachment of N-glycan to the Asn695 residue inhibits activity by disturbing electron transfer. N-glycosylated iNOS consumes NADPH more slowly than the unliganded enzyme. Mutating Asn695 to Gln695 yields an iNOS that exhibits greater enzyme activity compared to wild-type. NO produced by N695Q iNOS-transformed HEK293 cells is 1.32fold greater than that of N-glycosylated iNOS, the increased enzyme activity of N695Q iNOS in HEK293 cells was caused by loss of N-glycan |
-, 763831 |
| 1.14.13.39 | malfunction |
inhibition of NOS function by NOS inhibitor L-NG-monomethyl arginine (L-NMMA) results in reduced formation of mineralized nodules and expression of dentin sialophosphoprotein (DSPP) and dentin matrix protein (DMP1) during dental papilla cell (DPC) differentiation |
-, 764551 |
| 1.14.13.39 | malfunction |
role of oxidative stress in the dysfunction of the placental endothelial nitric oxide synthase in preeclampsia (PE), multifactorial pregnancy disease, characterized by new-onset gestational hypertension with (or without) proteinuria or end-organ failure, exclusively observed in humans. PE pathophysiology can result from abnormal placentation due to a defective trophoblastic invasion and an impaired remodeling of uterine spiral arteries, leading to a poor adaptation of utero-placental circulation. This would be associated with hypoxia/ reoxygenation phenomena, oxygen gradient fluctuations, altered antioxidant capacity, oxidative stress, and reduced nitric oxide (NO) bioavailability. This results in part from the reaction of NO with the radical anion superoxide, which produces peroxynitrite ONOO-, a powerful pro-oxidant and inflammatory agent. Another mechanism is the progressive inhibition of the placental endothelial nitric oxide synthase (eNOS) by oxidative stress, which results in eNOS uncoupling via several events such as a depletion of the eNOS substrate L-arginine due to increased arginase activity, an oxidation of the eNOS cofactor tetrahydrobiopterin (BH4), or eNOS posttranslational modifications (for instance by S-glutathionylation). The uncoupling of eNOS triggers a switch of its activity from a NO-producing enzyme to a NADPH oxidase-like system generating superoxide, thereby potentiating ROS production and oxidative stress. Moreover, in PE placentas, eNOS can be posttranslationally modified by lipid peroxidation-derived aldehydes such as 4-oxononenal (ONE) a highly bioreactive agent, able to inhibit eNOS activity and NO production. Analysis of the dysfunction of placental eNOS evoked by oxidative stress and lipid peroxidation products, and the potential consequences on PE pathogenesis, detailed overview. Oxidative stress is thought to play a pivotal role in the decreased NO bioavailability in PE pathophysiology, via several mechanisms including an inhibition of eNOS (eNOS uncoupling) and subsequent defect of NO biosynthesis, or through the formation of peroxynitrite, via the reaction of NO with the radical anion superoxide. eNOS inhibition is associated with a decrease in endothelial-dependent relaxation in vitro and in vivo. Therapeutic perspectives targeting oxidative stress and NO/eNOS dysfunction |
765745 |
| 1.14.13.39 | metabolism |
activation of G protein-coupled estrogen receptor in the supraoptic and paraventricular nuclei of the hypothalamus inhibits the phosphorylation of ERK 1/2, which induces a decrease in NADPH-diaphorase expression |
743357 |
| 1.14.13.39 | metabolism |
synthesis of the signaling molecule nitric oxide |
745379 |
| 1.14.13.39 | metabolism |
the enzyme plays an important role in host defense system by catalyzing the production of nitric oxide |
744948 |
| 1.14.13.39 | more |
residue Asn695 of the mouse iNOS locates at the hinge segment which connects the FMN-binding domain to the FAD-binding domain. The electrostatic and flexibility properties of hinge segment are critical for electron transfer from CPR to its redox partners. For mouse iNOS, N-glycosylation of Asn695 might disturb electron transfer by influencing the electrostatic and flexibility properties of the hinge segment |
-, 763831 |
| 1.14.13.39 | more |
the large numbers of nNOS neurons and the density of innervation of the circular muscle and pyloric sphincter suggest that there is a finely graded control of motor function in the stomach by the recruitment of different numbers of inhibitory motor neurons |
-, 764443 |
| 1.14.13.39 | physiological function |
developmental but not adult exposure to polychlorinated biphenyls significantly reduces NO synthase responses to hyperosmolality in neuroendocrine cells. Reduced NADPH diaphorase activity produced by in utero exposure persists in stimulated late adult rats concomitant with reduced osmoregulatory capacity |
743362 |
| 1.14.13.39 | physiological function |
during muscle pain development, a significant contralateral increase in the number of NADPH-diaphorase reactive cells is accompanied by anipsilateral increase in c-Fos expression in lamina VII. NADPH-diaphorase reactive neurons of the contralateral ventral horn may be involved through commissural connections in the maintenance of the neuronal activity associated with acute muscle inflammation. During acute myositis, plastic changes in the ventral horn may activate the processes of disinhibition due to an increase in the number of NADPH-diaphorase reactive neurons in the spinal gray matter |
741543 |
