Steady-State Kinetics of α-Synuclein Ferrireductase Activity Identifies the Catalytically Competent Species

Biochemistry

Volumn 56, Issue 19, 2017, Pages 2497-2505

  McDowall, Jennifer S ^a   Ntai, Ioanna ^a   Hake, Jonathon ^a   Whitley, Paul R ^a   Mason, Jody M ^a   Pudney, Christopher R ^a   Brown, David R ^a  

^a University of Bath   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; KINETICS; NEURODEGENERATIVE DISEASES; PROTEINS; RECOMBINANT PROTEINS;

ARTIFICIAL MEMBRANES; ASSOCIATED MECHANISM; CELLULAR REGULATION; CYTOSOLIC PROTEINS; ENZYMATIC ACTIVITIES; PARKINSON'S DISEASE; SECONDARY STRUCTURE FOLDING; STEADY-STATE KINETICS;

ENZYME ACTIVITY;

ALPHA SYNUCLEIN; FERROUS ION; OXIDOREDUCTASE; RECOMBINANT ALPHA SYNUCLEIN FERRIREDUCTASE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; FERRIC CITRATE IRON REDUCTASE; FLAVINE MONONUCLEOTIDE REDUCTASE; LIPOSOME; MEMBRANE PROTEIN; NANOMATERIAL; NERVE PROTEIN; RECOMBINANT PROTEIN;

ARTICLE; ARTIFICIAL MEMBRANE; CELL ASSAY; CONFORMATIONAL TRANSITION; DEGENERATIVE DISEASE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME STRUCTURE; ESCHERICHIA COLI; HUMAN; HUMAN CELL; NEUROBLASTOMA CELL LINE; NONHUMAN; OBSERVED RATE CONSTANT; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; REGULATORY MECHANISM; STEADY STATE; AMINO ACID SUBSTITUTION; BINDING SITE; BIOCATALYSIS; BIOLOGICAL MODEL; CHEMISTRY; COMPARATIVE STUDY; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR WEIGHT; MUTATION; NERVE CELL; SOLUBILITY; TUMOR CELL LINE;

ALPHA-SYNUCLEIN; AMINO ACID SUBSTITUTION; BINDING SITES; BIOCATALYSIS; CELL LINE, TUMOR; FMN REDUCTASE; HUMANS; LIPOSOMES; MEMBRANE PROTEINS; MODELS, BIOLOGICAL; MOLECULAR WEIGHT; MUTATION; NANOSTRUCTURES; NERVE TISSUE PROTEINS; NEURONS; RECOMBINANT PROTEINS; SOLUBILITY; SUBSTRATE SPECIFICITY;

EID: 85019427636     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.7b00257     Document Type: Article

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