Characterization of Ca2+ interactions with matrix metallopeptidase-12: Implications for matrix metallopeptidase regulation

Biochemical Journal

Volumn 398, Issue 3, 2006, Pages 393-398

  Gossas, Thomas ^a   Danielson, U Helena ^a  

^a UPPSALA UNIVERSITY   (Sweden)

Author keywords

Active conformation; Affinity; Calcium binding; Human macrophage elastase; Matrix metallopeptidase 12 (MMP 12); pH dependency

Indexed keywords

AFFINITY CHROMATOGRAPHY; BINDING ENERGY; CARBOXYLATION; CONFORMATIONS; ENZYME KINETICS; PH EFFECTS;

ACTIVE CONFORMATION; CALCIUM BINDING; HUMAN MACROPHAGE ELASTASE; MATRIX METALLOPEPTIDASE-12 (MMP-12);

ENZYMES;

ASPARTIC ACID; CALCIUM ION; CARBOXYLIC ACID; MACROPHAGE ELASTASE; ZINC ION; CALCIUM; METALLOPROTEINASE; MMP12 PROTEIN, HUMAN;

ARTICLE; BINDING AFFINITY; BINDING SITE; CALCIUM BINDING; CATALYSIS; CHEMICAL BINDING; ENZYME ACTIVITY; ENZYME STRUCTURE; HYDROLYSIS; ISOTHERM; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTON TRANSPORT; CHEMICAL STRUCTURE; ENZYME ACTIVATION; HUMAN; METABOLISM; PROTEIN BINDING;

CALCIUM; ENZYME ACTIVATION; HUMANS; HYDROGEN-ION CONCENTRATION; MATRIX METALLOPROTEINASE 12; METALLOENDOPEPTIDASES; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION;

EID: 33748749807     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20051933     Document Type: Article

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