Structural basis for activity regulation and substrate preference of clostridial collagenases G, H, and T

Journal of Biological Chemistry

Volumn 288, Issue 28, 2013, Pages 20184-20194

  Eckhard, Ulrich ^a,b   Schönauer, Esther ^a   Brandstetter, Hans ^a  

^a UNIVERSITY OF SALZBURG   (Austria)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVITY REGULATION; CALCIUM BINDING; COLLAGENOLYTIC ACTIVITIES; ENZYMATIC ACTIVITIES; INHIBITOR DESIGN; STRUCTURAL BASIS; SUBSTRATE SELECTIVITY; SUBSTRATE SPECIFICITY;

CALCIUM; ZINC;

ENZYMES;

ASPARTIC ACID; BACTERIAL ENZYME; CALCIUM ION; COLLAGENASE; COLLAGENASE G; COLLAGENASE H; COLLAGENASE T; ISOENZYME; UNCLASSIFIED DRUG; ZINC;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CLOSTRIDIUM HISTOLYTICUM; CLOSTRIDIUM TETANI; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME REGULATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; GENETIC CONSERVATION; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN QUATERNARY STRUCTURE; SEQUENCE HOMOLOGY;

COLLAGENASE; METAL REGULATION; PROTEASE; PROTEIN DEGRADATION; PROTEIN STRUCTURE; PROTEOLYTIC ENZYMES; X-RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BINDING SITES; BIOCATALYSIS; CALCIUM; CATALYTIC DOMAIN; CLOSTRIDIUM; CLOSTRIDIUM HISTOLYTICUM; ISOENZYMES; KINETICS; MICROBIAL COLLAGENASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEASE INHIBITORS; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; ZINC;

EID: 84880061207     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.448548     Document Type: Article

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