The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3

Journal of Biological Chemistry

Volumn 271, Issue 29, 1996, Pages 17119-17123

  Will, Horst ^a   Atkinson, Susan J ^b   Butler, Georgina S ^b   Smith, Bryan ^c   Murphy, Gillian ^b  

^a InViTek GmbH   (Germany)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^c UCB PHARMA   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGENASE; ENZYME PRECURSOR; GELATINASE; MUTANT PROTEIN; TISSUE INHIBITOR OF METALLOPROTEINASE;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME REGULATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN PROCESSING;

AMINO ACID SEQUENCE; ASPARAGINE; BINDING SITES; CATALYSIS; CLONING, MOLECULAR; COLLAGENASES; ENZYME ACTIVATION; ENZYME PRECURSORS; GELATINASES; HUMANS; KINETICS; LEUCINE; MATRIX METALLOPROTEINASE 1; METALLOENDOPEPTIDASES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDE FRAGMENTS; POINT MUTATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEINS; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; TISSUE INHIBITOR OF METALLOPROTEINASE-2; TISSUE INHIBITOR OF METALLOPROTEINASE-3; TYROSINE;

EID: 0030016342     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.29.17119     Document Type: Article

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