A conserved domain in prokaryotic bifunctional FAD synthetases can potentially catalyze nucleotide transfer

Trends in Biochemical Sciences

Volumn 28, Issue 1, 2003, Pages 9-12

  Krupa, Ananth ^a   Sandhya, Kumaraswamy ^b   Srinivasan, Narayanaswamy ^a   Jonnalagadda, Sobhanaditya ^b  

^a INDIAN INSTITUTE OF SCIENCE   (India)

^b OSMANIA UNIVERSITY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; ENZYME; FLAVINE ADENINE NUCLEOTIDE SYNTHETASE; FLAVINE MONONUCLEOTIDE; NUCLEOTIDYLTRANSFERASE; UNCLASSIFIED DRUG;

ADENYLATION; AMINO TERMINAL SEQUENCE; CATALYSIS; ENZYME ACTIVITY; ENZYME BINDING; ENZYME SYNTHESIS; NONHUMAN; NUCLEOTIDE SEQUENCE; NUCLEOTIDE TRANSPORT; PHOSPHORYLATION; PRIORITY JOURNAL; PROKARYOTE; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN MOTIF; REVIEW; SEQUENCE ANALYSIS;

BACTERIA (MICROORGANISMS); PROKARYOTA;

EID: 0037219142     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(02)00009-9     Document Type: Short Survey

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