Transition states of uncatalyzed hydrolysis and aminolysis reactions of a ribosomal p-site substrate determined by kinetic isotope effects

Biochemistry

Volumn 49, Issue 18, 2010, Pages 3868-3878

  Hiller, David A ^a   Zhong, Minghong ^a   Singh, Vipender ^a   Strobel, Scott A ^a  

^a YALE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

[CARBONYL; AMINOLYSIS; AMINOLYSIS REACTION; CATALYZED REACTIONS; DEUTERIUM EFFECT; ESTER BONDS; ISOTOPE EFFECT; KINETIC ISOTOPE EFFECTS; LEAVING GROUPS; NUCLEOPHILIC ATTACK; PEPTIDE BONDS; PEPTIDE RELEASE; RATE ENHANCEMENT; TRANSITION STATE; TRANSITION STATE STRUCTURE; UNCATALYZED HYDROLYSIS; UNCATALYZED REACTIONS;

CARBONYLATION; DEUTERIUM; ESTERS; HYDROLYSIS; PEPTIDES; REACTION KINETICS;

CARRIER MOBILITY;

CARBONYL DERIVATIVE; DEUTERIUM; ESTER; HYDROXYLAMINE; ISOTOPE; TRANSFER RNA;

AMINOLYSIS; ARTICLE; CATALYSIS; CHEMICAL BOND; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME STRUCTURE; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN SECRETION; RIBOSOME; SUBSTITUTION REACTION;

HYDROLYSIS; HYDROXYLAMINE; KINETICS; MODELS, CHEMICAL; MOLECULAR STRUCTURE; RIBOSOMES; RNA, TRANSFER, AMINO ACYL; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

EID: 77951932920     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi901458x     Document Type: Article

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