Tyr219 of human matrix metalloproteinase 7 is not critical for catalytic activity, but is involved in the broad pH-dependence of the activity

Journal of Biochemistry

Volumn 150, Issue 2, 2011, Pages 183-188

  Muta, Yuko ^a   Inouye, Kuniyo ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

matrix metalloproteinase; MMP 7; pH activity profile; site directed mutagenesis; tyrosyl residue

Indexed keywords

MATRILYSIN; TYROSINE;

ARTICLE; CATALYSIS; ENZYME ACTIVITY; HYDROLYSIS; PH; SITE DIRECTED MUTAGENESIS;

CATALYSIS; CATALYTIC DOMAIN; HUMANS; HYDROGEN-ION CONCENTRATION; MATRIX METALLOPROTEINASE 7; MUTAGENESIS, SITE-DIRECTED; MUTATION; OLIGOPEPTIDES; PROTEIN CONFORMATION; TYROSINE;

EID: 79961090772     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvr050     Document Type: Article

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