Protein interactions in the human methionine synthase-methionine synthase reductase complex and implications for the mechanism of enzyme reactivation
about
Concept mapping One-Carbon Metabolism to model future ontologies for nutrient-gene-phenotype interactions.A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanismNADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family.Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthaseDistinct conformational behaviors of four mammalian dual-flavin reductases (cytochrome P450 reductase, methionine synthase reductase, neuronal nitric oxide synthase, endothelial nitric oxide synthase) determine their unique catalytic profiles.A conformational sampling model for radical catalysis in pyridoxal phosphate- and cobalamin-dependent enzymes.Genetic polymorphisms involved in folate metabolism and maternal risk for down syndrome: a meta-analysisA kinetic model linking protein conformational motions, interflavin electron transfer and electron flux through a dual-flavin enzyme-simulating the reductase activity of the endothelial and neuronal nitric oxide synthase flavoprotein domains.Control of electron transfer and catalysis in neuronal nitric-oxide synthase (nNOS) by a hinge connecting its FMN and FAD-NADPH domains.Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins.Kinetics of reversible reductive carbonylation of heme in human cystathionine β-synthase.Restricted role for methionine synthase reductase defined by subcellular localization.Charge-pairing interactions control the conformational setpoint and motions of the FMN domain in neuronal nitric oxide synthase.The tinker, tailor, soldier in intracellular B12 trafficking.Orchestrated Domain Movement in Catalysis by Cytochrome P450 Reductase.Docking analysis of transient complexes: interaction of ferredoxin-NADP+ reductase with ferredoxin and flavodoxin.Phosphorylation Controls Endothelial Nitric-oxide Synthase by Regulating Its Conformational Dynamics.Bacterial Production, Characterization and Protein Modeling of a Novel Monofuctional Isoform of FAD Synthase in Humans: An Emergency Protein?Defective MTRR does not convert cob(II)alamin to MeCblcob(II)alamin binds to MTRR:MTRMTRR reduces cob(II)alamin to meCblCobalamin uptake and reactivation occurs through specific protein interactions in the methionine synthase-methionine synthase reductase complex.ELDOR Spectroscopy Reveals that Energy Landscapes in Human Methionine Synthase Reductase are Extensively Remodelled Following Ligand and Partner Protein Binding
P2860
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P2860
Protein interactions in the human methionine synthase-methionine synthase reductase complex and implications for the mechanism of enzyme reactivation
description
2007 nî lūn-bûn
@nan
2007 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Protein interactions in the hu ...... chanism of enzyme reactivation
@ast
Protein interactions in the hu ...... chanism of enzyme reactivation
@en
Protein interactions in the hu ...... chanism of enzyme reactivation
@nl
type
label
Protein interactions in the hu ...... chanism of enzyme reactivation
@ast
Protein interactions in the hu ...... chanism of enzyme reactivation
@en
Protein interactions in the hu ...... chanism of enzyme reactivation
@nl
prefLabel
Protein interactions in the hu ...... chanism of enzyme reactivation
@ast
Protein interactions in the hu ...... chanism of enzyme reactivation
@en
Protein interactions in the hu ...... chanism of enzyme reactivation
@nl
P356
P1433
P1476
Protein interactions in the hu ...... chanism of enzyme reactivation
@en
P2093
Kirsten R Wolthers
Nigel S Scrutton
P304
P356
10.1021/BI700339V
P407
P577
2007-06-12T00:00:00Z