Adenylyl cyclase Rv0386 from Mycobacterium tuberculosis H37Rv uses a novel mode for substrate selection

FEBS Journal

Volumn 272, Issue 12, 2005, Pages 3085-3092

  Castro, Lucila I ^a   Hermsen, Corinna ^a   Schultz, Joachim E ^a   Linder, Jürgen U ^a  

^a UNIVERSITY OF TÜBINGEN   (Germany)

Author keywords

Adenylyl cyclase; Cyclic nucleotide; Mycobacterium tuberculosis; Quanylyl cyclase; Substrate specificity

Indexed keywords

ADENINE; ADENOSINE TRIPHOSPHATASE; ADENYLATE CYCLASE; ASPARAGINE; ASPARTIC ACID; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; GLUTAMINE; HELIX LOOP HELIX PROTEIN; LYSINE; PURINE; RECOMBINANT ENZYME;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIAL GENE; BACTERIAL GENOME; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME SPECIFICITY; GENE FUSION; GENE MUTATION; GENETIC CONSERVATION; MYCOBACTERIUM TUBERCULOSIS; MYCOBACTERIUM TUBERCULOSIS H37RV; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DOMAIN;

ADENOSINE TRIPHOSPHATE; ADENYLATE CYCLASE; AMINO ACID SEQUENCE; ASPARAGINE; CATALYTIC DOMAIN; GLUTAMINE; GUANOSINE TRIPHOSPHATE; ISOENZYMES; MOLECULAR SEQUENCE DATA; MUTATION; MYCOBACTERIUM TUBERCULOSIS; SUBSTRATE SPECIFICITY;

MYCOBACTERIUM TUBERCULOSIS;

EID: 21344433227     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04722.x     Document Type: Article

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