Anomalous pH-dependence of the activity of human matrilysin (matrix metalloproteinase-7) as revealed by nitration and amination of its tyrosine residues

Biochemical Journal

Volumn 386, Issue 2, 2005, Pages 263-270

  Muta, Yuko ^a   Oneda, Hiroshi ^a   Inouye, Kuniyo ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

Enzyme activity; Matrilysin; Matrix metalloproteinase; Nitrotyrosine; pH dependence; Tyrosine residue

Indexed keywords

ACIDITY; ALKALINITY; AMINATION; IONIZATION; NITRATION; PH EFFECTS;

MATRILYSIN ACTIVITY; MICHAELIS CONSTANTS; NITROTYROSINE; TYROSINES;

ENZYMES;

MATRILYSIN;

AMINATION; ARTICLE; ENZYME ACTIVITY; ENZYME MODIFICATION; MICHAELIS CONSTANT; NITRATION; PH; PKA; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

2,4-DINITROPHENOL; AMINATION; AMINO ACIDS, ACIDIC; AZO COMPOUNDS; CATALYSIS; CIRCULAR DICHROISM; COLLAGEN; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MATRIX METALLOPROTEINASE 7; MUTAGENESIS, SITE-DIRECTED; OLIGOPEPTIDES; PLASMINOGEN; RECOMBINANT PROTEINS; TRANSAMINASES; TYROSINE;

EID: 14844302862     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040985     Document Type: Article

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