Relationships between the calmodulin-dependent adenylate cyclases produced by Bacillus anthracis and Bordetella pertussis.
The nucleotide sequences for the calmodulin-dependent adenylate cyclases produced by Bordetella pertussis and Bacillus anthracis have recently been determined. The GC% for the B. pertussis and B. anthracis cyclase genes are about 65% and 29%, respectively. Despite this difference in nucleotide composition, these cyclases possess three highly conserved amino acid domains and share some nucleotide sequence homology. One of these conserved domains appears to be involved in ATP binding and is related to the consensus amino acid sequences present in many eukaryotic and prokaryotic ATP and GTP binding proteins. The possible relationship between these cyclases and eukaryotic calmodulin-dependent adenylate cyclases is discussed.
Robertson
D L
DL
Department of Chemistry, Brigham Young University, Provo, UT 84602.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000262:Adenylyl Cyclases / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D001408:Bacillus anthracis / Q000201:enzymology* / Q000235:genetics; D001482:Base Composition; D001483:Base Sequence; D001665:Binding Sites; D001886:Bordetella pertussis / Q000201:enzymology* / Q000235:genetics; D002147:Calmodulin / Q000378:metabolism / Q000494:pharmacology*; D004269:DNA, Bacterial / Q000032:analysis; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid
D002147:Calmodulin; D004269:DNA, Bacterial; D000255:Adenosine Triphosphate; D000262:Adenylyl Cyclases