Matrix metalloproteinase triple-helical peptidase activities are differentially regulated by substrate stability

Biochemistry

Volumn 43, Issue 36, 2004, Pages 11474-11481

  Minond, Dmitriy ^a   Lauer Fields, Janelle L ^a   Nagase, Hideaki ^b   Fields, Gregg B ^a  

^a FLORIDA ATLANTIC UNIVERSITY   (United States)

^b IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGENOLYTIC SPECIFICITY; PEPTIDASE ACTIVITY;

ACTIVATION ENERGY; COLLAGEN; ENZYMES; HYDROLYSIS; PATHOLOGY; PHYSIOLOGICAL MODELS; TISSUE;

BIOCHEMISTRY;

BENZYL DERIVATIVE; COLLAGEN; COLLAGEN TYPE 1; COLLAGEN TYPE 2; COLLAGEN TYPE 3; CYSTEINE DERIVATIVE; INTERSTITIAL COLLAGENASE; LEUCINE; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 14; PEPTIDASE; TRIPLE HELICAL PEPTIDASE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CHEMICAL MODEL; CIRCULAR DICHROISM; CONSENSUS CLEAVAGE SITE; CONSENSUS SEQUENCE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME SPECIFICITY; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMOSTABILITY; TRIPLE HELIX;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; COLLAGEN TYPE I; COLLAGEN TYPE II; COLLAGEN TYPE III; ENZYME ACTIVATION; ENZYME STABILITY; EXOPEPTIDASES; FLUORESCENT DYES; HUMANS; HYDROLYSIS; MATRIX METALLOPROTEINASES, MEMBRANE-ASSOCIATED; METALLOENDOPEPTIDASES; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; SUBSTRATE SPECIFICITY; TEMPERATURE;

EID: 4444290999     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048938i     Document Type: Article

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