rapid and specific microplate assay to monitor MsrA activity based on oxidation of dithiothreitol, whose color can be produced by reacting with Ellman's reagent
with MsrA adsorbed on glassy carbon and boron doped diamond electrodes surface, the first step reaction step corresponds to the oxidation of tyrosine and tryptophan residues and occurs for the same potential. The second step is histidine oxidation, and the third, at higher potentials, the second tryptophan oxidation. MsrA adsorbs on the hydrophobic carbon electrode surface preferentially through the three hydrophobic domains, C1, C2 and C3, which contain the tyrosine, tryptophan and histidine residues
interventions focusing on the enzymatic reduction of oxidized methionine catalyzed by MSRA represents a new prevention and therapeutic approach for Parkinsons disease and potentially for other neurodegenerative diseases involving oxidative stress
MsrA efficiently reduces oxidized methionine residues in recombinant alpha-synuclein. Enhancing MsrA function may be a reasonable therapeutic strategy in Parkinson's disease
Caenorhabditis elegans model of the human amyloidogenic disease inclusion body myositis. In a constitutive transgenic Abeta strain that lacks MSRA-1, the number of amyloid aggregates decreases while the number of oligomeric Abeta species increases. The results correlate with enhanced synaptic dysfunction and mislocalization of the nicotinic acetylcholine receptor ACR-16 at the neuromuscular junction
mouse model of Alzheimer's disease, a mouse that overexpresses amyloid precursor protein and Abeta in neurons. Lack of MsrA fosters the formation of methionine sulfoxide in proteins. MsrA-deficient mice expressing amyloid precursor protein exhibit higher levels of soluble Abeta in brain. Mitochondrial respiration and the activity of cytochrome c oxidase are compromised in the MsrA-deficient mice expressing amyloid precursor protein compared with control mice
reductive resolution for the synthesis of optically active sulfoxides. Whole-cell system expressing recombinant pmMsrA protein is designed for the preparation of chiral sulfoxides with R configuration through reductive resolution of racemic sulfoxides
the enzyme can effectively accomplish the preparation of (R)-sulfoxides with approximately 50% yield and 94-99% enantiomeric excess through asymmetric reductive resolution of racemic sulfoxide. With the establishment of the enzyme regeneration system, the initial substrate concentration can be increased 40-100times. The (R)-sulfoxides are obtained with high enantioselectivity under the substrate concentration up to 200 mm (approximately 32 g/L), representing a quite high substrate concentration in biocatalytic preparation of chiral sulfoxides. This system shows fairly good activity and enantioselectivity towards a series of ortho- and para-substituted phenyl methyl sulfoxides under high substrate concentration
the study supports that the asymmetric reductive resolution of rac-sulfoxides using MsrA would become an effective strategy for the green synthesis of optically pure sulfoxides
the enzyme can effectively accomplish the preparation of (R)-sulfoxides with approximately 50% yield and 94-99% enantiomeric excess through asymmetric reductive resolution of racemic sulfoxide. With the establishment of the enzyme regeneration system, the initial substrate concentration can be increased 40-100times. The (R)-sulfoxides are obtained with high enantioselectivity under the substrate concentration up to 200 mm (approximately 32 g/L), representing a quite high substrate concentration in biocatalytic preparation of chiral sulfoxides. This system shows fairly good activity and enantioselectivity towards a series of ortho- and para-substituted phenyl methyl sulfoxides under high substrate concentration
reductive resolution for the synthesis of optically active sulfoxides. Whole-cell system expressing recombinant pmMsrA protein is designed for the preparation of chiral sulfoxides with R configuration through reductive resolution of racemic sulfoxides