A naturally occurring nonapeptide functionally compensates for the CP1 domain of leucyl-tRNA synthetase to modulate aminoacylation activity

Biochemical Journal

Volumn 443, Issue 2, 2012, Pages 477-484

  Tan, Min ^a   Yan, Wei ^a   Liu, Ru Juan ^a   Wang, Meng ^a   Chen, Xin ^a   Zhou, Xiao Long ^a   Wang, En Duo ^a  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

Author keywords

Aminoacylation; CP1 (connective peptide 1) domain; Evolution; Leucyl tRNA synthetase; RNA editing

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; LEUCINE TRANSFER RNA LIGASE; NONAPEPTIDE;

AMINOACYLATION; AQUIFEX AEOLICUS; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ESCHERICHIA COLI; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; AMINOACYLATION; BIOCATALYSIS; LEUCINE-TRNA LIGASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MYCOPLASMA; PEPTIDES; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT;

AQUIFEX AEOLICUS; ESCHERICHIA COLI; MYCOPLASMA MOBILE;

EID: 84859451220     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20111925     Document Type: Article

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