Lysyl-tRNA synthetase-generated lysyl-adenylate is a substrate for histidine triad nucleotide binding proteins

Journal of Biological Chemistry

Volumn 282, Issue 7, 2007, Pages 4719-4727

  Chou, Tsui Fen ^a   Wagner, Carston R ^a,b  

^a UNIVERSITY OF MINNESOTA   (United States)

^b University of Minnesota   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HISTIDINE TRIAD NUCLEOTIDE BINDING PROTEINS (HINTS); HISTIDINE TRIAD PROTEINS; HYDROLYASES; NUCLEOTIDYLTRANSFERASES;

BINDING SITES; COMPLEXATION; MUTAGENESIS; NUCLEOTIDES; PROTEINS; RNA;

ENZYME KINETICS;

ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID TRANSFER RNA LIGASE; GUANOSINE TRIPHOSPHATE; HISTIDINE TRIAD NUCLEOTIDE BINDING PROTEIN; LYSINE; LYSINE TRANSFER RNA LIGASE; LYSYL ADENOSINE PHOSPHATE; MAGNESIUM; NUCLEOTIDE BINDING PROTEIN; PHOSPHORUS 32; UNCLASSIFIED DRUG; ZINC; DRUG DERIVATIVE; ESCHERICHIA COLI PROTEIN; HINT1 PROTEIN, HUMAN; INORGANIC PYROPHOSPHATASE; LYSYLADENYLATE; MICROPHTHALMIA ASSOCIATED TRANSCRIPTION FACTOR; MITF PROTEIN, HUMAN; NERVE PROTEIN; UPSTREAM STIMULATORY FACTOR; USF2 PROTEIN, HUMAN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BIOCHEMISTRY; CONCENTRATION (PARAMETERS); ENZYME SUBSTRATE; ESCHERICHIA COLI; HUMAN; ISOTOPE LABELING; KINETICS; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

ESCHERICHIA COLI;

ADENOSINE MONOPHOSPHATE; AMINO ACID SUBSTITUTION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HUMANS; LYSINE-TRNA LIGASE; MICROPHTHALMIA-ASSOCIATED TRANSCRIPTION FACTOR; MUTAGENESIS, SITE-DIRECTED; NERVE TISSUE PROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PYROPHOSPHATASES; UPSTREAM STIMULATORY FACTORS;

EID: 33947523522     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M610530200     Document Type: Article

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