Slight sequence variations of a common fold explain the substrate specificities of tRNA-guanine transglycosylases from the three kingdoms

FEBS Letters

Volumn 416, Issue 1, 1997, Pages 93-98

  Romier, Christophe ^a   Meyer, Joachim E W ^a   Suck, Dietrich ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Arachaeosine; Catalytic mechanism; Homology; Modeling; Queuine; tRNA guanine transglycosylase

Indexed keywords

GLYCOSYLTRANSFERASE; QUEUINE TRANSFER RIBONUCLEIC ACID RIBOSYLTRANSFERASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARCHAEBACTERIUM; ARTICLE; CONTROLLED STUDY; ENZYME SPECIFICITY; HUMAN; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ARCHAEA; EUKARYOTIC CELLS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PENTOSYLTRANSFERASES; PROKARYOTIC CELLS; PROTEIN FOLDING; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY;

ARCHAEA; EUKARYOTA; PROKARYOTA;

EID: 0030832831     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(97)01175-7     Document Type: Article

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