Search results for "Flavin mononucleotide"

showing 3 items of 3 documents

Expression and Expressional Control of Nitric Oxide Synthases in Various Cell Types

1995

Publisher Summary Nitric oxide (NO) can produce posttranslational modifications of proteins (via ADP ribosylation) and is capable of destroying parasites and tumor cells by inhibiting iron-containing enzymes or directly interacting with the DNA of these cells. In view of this multitude of functions of NO, it is important to understand how cells accomplish and regulate their NO production. Three isozymes of NOS have been identified, and their protein, cDNA, and genomic DNA structures have been elucidated. In humans NOS I, II, and III are encoded by three different genes, located on chromosomes 12, 17, and 7 respectively. The cDNAs for these enzymes have been isolated. All NOS isozymes oxidiz…

chemistry.chemical_classificationGene isoformbiologyFlavin mononucleotideIsozymeCofactorNitric oxidechemistry.chemical_compoundEnzymeBiochemistrychemistryComplementary DNAbiology.proteinDNA
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Post-Translational Regulation of CYP450s Metabolism As Revealed by All-Atoms Simulations of the Aromatase Enzyme.

2019

Phosphorylation by kinases enzymes is a widespread regulatory mechanism able of rapidly altering the function of target proteins. Among these are cytochrome P450s (CYP450), a superfamily of enzymes performing the oxidation of endogenous and exogenous substrates thanks to the electron supply of a redox partner. In spite of its pivotal role, the molecular mechanism by which phosphorylation modulates CYP450s metabolism remains elusive. Here by performing microsecond-long all-atom molecular dynamics simulations, we disclose how phosphorylation regulates estrogen biosynthesis, catalyzed by the Human Aromatase (HA) enzyme. Namely, we unprecedentedly propose that HA phosphorylation at Y361 markedl…

CytochromeFlavin MononucleotideProtein ConformationGeneral Chemical EngineeringFlavin mononucleotide-Oxidative phosphorylationLibrary and Information SciencesMolecular Dynamics Simulation01 natural scienceschemistry.chemical_compoundAromatase0103 physical sciencesPost-translational regulationAromatasePhosphorylationBinding Sites010304 chemical physicsbiologyKinaseGeneral ChemistryMetabolism0104 chemical sciencesComputer Science ApplicationsCell biology010404 medicinal & biomolecular chemistrychemistrySettore CHIM/03 - Chimica Generale E Inorganicabiology.proteinFlavin-Adenine DinucleotidePhosphorylationQuantum TheoryProtein Processing Post-TranslationalNADPJournal of chemical information and modeling
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[26] Isoforms of nitric-oxide synthase: Purification and regulation

1994

Publisher Summary Nitric-oxide synthase (NOS) catalyzes the five-electron oxidation of L-arginine to the nitric oxide radical (.NO) and L-citrulline. Molecular oxygen is the cosubstrate of the enzyme. NO synthase activity has been found in a large variety of cells and tissues. The enzyme exists in several isoforms, three of which have been purified, characterized, and cloned. The activities of all three isoforms are found distributed between the soluble and particulate fractions of cells. Isoform I (from brain) and isoform II (from cytokine-induced macrophages) are mostly soluble proteins. Isoform III from endothelial cells is myristoylated and found predominantly in the particulate fractio…

Flavin adenine dinucleotideGene isoformATP synthasebiologyFlavin mononucleotideFlavin groupIsozymeMolecular biologyCofactorNitric oxide synthasechemistry.chemical_compoundchemistryBiochemistrybiology.protein
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