Mutagenesis of three residues, isoleucine-60, threonine-61, and aspartic acid-80, implicated in the GTPase activity of Escherichia coli elongation factor TU

Biochemistry

Volumn 38, Issue 40, 1999, Pages 13035-13041

  Krab, Ivo M ^a   Parmeggiani, Andrea ^a  

^a ECOLE POLYTECHNIQUE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOACYL TRANSFER RNA; ASPARTIC ACID; ELONGATION FACTOR TU; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; ISOLEUCINE; MAGNESIUM ION; MOCIMYCIN; MUTANT PROTEIN; THREONINE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING KINETICS; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME REGULATION; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN NUCLEIC ACID INTERACTION; PROTEIN RNA BINDING; RIBOSOME; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

ASPARTIC ACID; BINDING SITES; ESCHERICHIA COLI; ESTERS; GTP PHOSPHOHYDROLASES; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; ISOLEUCINE; MAGNESIUM; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PEPTIDE ELONGATION FACTOR TU; PEPTIDES; PYRIDONES; RECOMBINANT PROTEINS; RIBOSOMES; RNA, TRANSFER, PHE; THREONINE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0032878323     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9909748     Document Type: Article

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