Two conserved threonines collaborate in the Escherichia coli Leucyl-tRNA synthetase amino acid editing mechanism

Biochemistry

Volumn 44, Issue 47, 2005, Pages 15437-15443

  Zhai, Yuxin ^a   Martinis, Susan A ^a,b  

^a University of Houston   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CRYSTAL STRUCTURE; ESCHERICHIA COLI; MUTAGENESIS; PROTEINS; RNA;

AMINO ACID EDITING; CRITICAL AMINO ACIDS; PROTEIN SYNTHESIS; TRANSITION STATE;

ENZYMES;

AMINO ACID; HYDROXYL GROUP; ISOLEUCINE TRANSFER RNA LIGASE; LEUCINE TRANSFER RNA LIGASE; THREONINE; TRANSFER RNA; VALINE TRANSFER RNA LIGASE;

ARTICLE; COVALENT BOND; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; GENE DELETION; GENE MUTATION; GENETIC CONSERVATION; MOLECULAR STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN SYNTHESIS; RNA EDITING;

ACYLATION; BINDING SITES; CONSERVED SEQUENCE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; LEUCINE-TRNA LIGASE; MUTATION; RNA EDITING; THERMODYNAMICS; THREONINE;

ESCHERICHIA COLI;

EID: 28244498723     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0514461     Document Type: Article

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