Influence of charge distribution at the active site surface on the substrate specificity of human neutrophil protease 3 and elastase: A kinetic and molecular modeling analysis

Journal of Biological Chemistry

Volumn 282, Issue 3, 2007, Pages 1989-1997

  Korkmaz, Brice ^a,b   Hajjar, Eric ^c   Kalupov, Timofey ^a,b   Reuter, Nathalie ^c   Brillard Bourdet, Michèle ^a,b   Moreau, Thierry ^a,b   Juliano, Luiz ^d   Gauthier, Francis ^a,b  

^a INSERM   (France)

^b UNIVERSITÉ DE TOURS   (France)

^c UNIVERSITY OF BERGEN   (Norway)

^d FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE SURFACE; BIOLOGICAL FUNCTIONS; ELECTROSTATIC SURFACE POTENTIAL; FLUORESCENCE RESONANCE ENERGY TRANSFER; NEUTROPHIL PROTEASE; PROTEIN SEQUENCE; PUTATIVE PROTEIN; SUBSTRATE SPECIFICITY;

CHARGE DISTRIBUTION; ENZYME INHIBITION; MOLECULAR MODELING; PHYSIOLOGY; SUBSTRATES; SURFACE POTENTIAL;

ENZYME KINETICS;

CELL ENZYME; ELASTASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PEPTIDE; PROTEASE 3; PROTEIN P21; UNCLASSIFIED DRUG; CYCLIN DEPENDENT KINASE INHIBITOR 1A; INTERLEUKIN 18; MYELOBLASTIN; PANCREATIC ELASTASE;

AMINO ACID SEQUENCE; ARTICLE; CELL SURFACE; CONSENSUS SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME DEGRADATION; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME SUBSTRATE; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN; HUMAN CELL; HYDROLYSIS; MOLECULAR DYNAMICS; MOLECULAR MODEL; NEUTROPHIL; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN HYDROLYSIS; SEQUENCE ANALYSIS; SIMULATION; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ELECTRICITY; KINETICS; METABOLISM; MOLECULAR GENETICS; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BINDING SITES; CYCLIN-DEPENDENT KINASE INHIBITOR P21; ELECTROSTATICS; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMANS; INTERLEUKIN-18; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MYELOBLASTIN; NF-KAPPA B; PANCREATIC ELASTASE; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EID: 33847265882     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M608700200     Document Type: Article

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