The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction

EMBO Journal

Volumn 16, Issue 18, 1997, Pages 5562-5571

  Jaggi, Rene ^a   Van Heeswijk, Wally C ^b   Westerhoff, Hans V ^b   Ollis, David L ^c   Vasudevan, Subhash G ^a  

^a JAMES COOK UNIVERSITY   (Australia)

^b VU UNIVERSITY AMSTERDAM   (Netherlands)

^c AUSTRALIAN NATIONAL UNIVERSITY   (Australia)

Author keywords

Escherichia coli adenylyl transferase; Flexible linker; Intramolecular signal transduction; Nucleotidyl transferase; PII protein

Indexed keywords

2 OXOGLUTARIC ACID; BACTERIAL ENZYME; GLUTAMATE AMMONIA LIGASE; TRANSFERASE;

ADENYLATION; AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME PURIFICATION; ESCHERICHIA COLI; NITROGEN FIXATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; CATALYSIS; ESCHERICHIA COLI; GENOTYPE; GLUTAMATE-AMMONIA LIGASE; KINETICS; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; NUCLEOTIDYLTRANSFERASES; PEPTIDE FRAGMENTS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SIGNAL TRANSDUCTION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0030880188     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.18.5562     Document Type: Article

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