The amino-acid substituents of dipeptide substrates of cathepsin C can determine the rate-limiting steps of catalysis

Biochemistry

Volumn 51, Issue 38, 2012, Pages 7551-7568

  Rubach, Jon K ^a,b   Cui, Guanglei ^a   Schneck, Jessica L ^a   Taylor, Amy N ^a   Zhao, Baoguang ^a   Smallwood, Angela ^a   Nevins, Neysa ^a   Wisnoski, David ^a   Thrall, Sara H ^a   Meek, Thomas D ^a  

^a GLAXOSMITHKLINE   (United States)

^b Kemin Industries Inc   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SUBSTRATES; CONFORMATIONAL FREEDOM; CRYSTALLOGRAPHIC STUDIES; CYSTEINE PROTEASE; DEACYLATION; DIPEPTIDE; DRUG DISCOVERY; FAST TRANSIENTS; FITTED VALUES; HALF-REACTIONS; INHIBITOR DESIGN; KINETIC DATA; KINETIC MODELING; KINETIC MODELS; KINETIC PROFILES; KINETIC STUDY; OPTIMAL ALIGNMENTS; PRE-STEADY-STATE KINETIC METHODS; RATE-LIMITING STEPS; RELATIVE RATES; SOLVENT KINETIC ISOTOPE EFFECTS; SUBSTRATE TYPES; THIOLATION; TIME COURSE; TRANSIENT PHASE;

ACYLATION; AMINO ACIDS; CARRIER MOBILITY; CATALYSIS; CHEMICAL ANALYSIS; ENZYME ACTIVITY; HYDROLYSIS; ISOTOPES; KINETIC THEORY; KINETICS; MOLECULAR DYNAMICS; PEPTIDES; REACTION INTERMEDIATES; REACTION KINETICS;

SUBSTRATES;

AMINO ACID; ARGININE; DIPEPTIDE DERIVATIVE; DIPEPTIDYL PEPTIDASE I; GLYCINE; ISOTOPE; SERINE; TYROSINE;

ACYLATION; ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTALLOGRAPHY; DEACYLATION; HYDROLYSIS; KINETICS; MOLECULAR DYNAMICS; MOLECULAR MODEL; PRIORITY JOURNAL; STEADY STATE;

AMINO ACIDS; CATALYSIS; CATHEPSIN C; DIPEPTIDES; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR DYNAMICS SIMULATION; SUBSTRATE SPECIFICITY;

EID: 84866692512     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300719b     Document Type: Article

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