Role of low-molecular-weight substrates in functional binding of the tRNAPhe acceptor end by phenylalanyl-tRNA synthetase

Biochemistry (Moscow)

Volumn 69, Issue 2, 2004, Pages 143-153

  Vasil'eva, I A ^a   Bogachev, V S ^a   Favre, A ^b   Lavrik, O I ^a   Moor, N A ^a  

^a INSTITUTE OF CHEMICAL BIOLOGY AND FUNDAMENTAL MEDICINE   (Russian Federation)

^b INSTITUT JACQUES MONOD   (France)

Author keywords

4 thiouridine; Acceptor end; Affinity modification; Phenylalanyl tRNA synthetase; Thermus thermophilus; tRNA

Indexed keywords

BIOCHEMISTRY; COMPLEXATION; ENZYMES; METHANATION; RNA; TOPOLOGY;

AFFINITY MODIFICATION; THERMUS THERMOPHILUS; TRNA;

MOLECULAR WEIGHT;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA; THERMUS; THERMUS THERMOPHILUS;

BACTERIAL PROTEIN; PHENYLALANINE TRANSFER RNA; PHENYLALANINE TRANSFER RNA LIGASE; THIOURIDINE;

ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; HUMAN; KINETICS; METABOLISM; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; THERMUS THERMOPHILUS;

BACTERIAL PROTEINS; BINDING SITES; ESCHERICHIA COLI; HUMANS; KINETICS; MODELS, MOLECULAR; PHENYLALANINE-TRNA LIGASE; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RNA, TRANSFER, PHE; SEQUENCE HOMOLOGY; SUBSTRATE SPECIFICITY; THERMUS THERMOPHILUS; THIOURIDINE;

EID: 3543049065     PISSN: 00062979     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:BIRY.0000018944.53390.44     Document Type: Article

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