Structural and functional relationships between Pasteurella multocida and enterobacterial adenylate cyclases

The Pasteurella multocida adenylate cyclase gene has been cloned and expressed in Escherichia coli. The primary structure of the protein (838 amino acids) deduced from the corresponding nucleotide sequence was compared with that of E. coli. The two enzymes have similar molecular sizes and, based on...

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Bibliographic Details
Published in:Journal of Bacteriology 1991-10, Vol.173 (19), p.6265-6269
Main Authors: Mock, M. (Institut Pasteur, Paris, France), Crasnier, M, Duflot, E, Dumay, V, Danchin, A
Format: Article
Language:English
Subjects:
activity
ADENILATO CICLASA
ADENYLATE CYCLASE
Adenylyl Cyclases - chemistry
Adenylyl Cyclases - genetics
Amino Acid Sequence
Bacteriology
Base Sequence
Biological and medical sciences
Cloning, Molecular
cya gene
Enterobacteriaceae - enzymology
Enterobacteriaceae - genetics
ESCHERICHIA
Escherichia coli
Escherichia coli - genetics
EXPRESION GENICA
EXPRESSION DES GENES
Fundamental and applied biological sciences. Psychology
GENE
Gene Expression Regulation, Bacterial
GENES
Genes, Bacterial
homology
Metabolism. Enzymes
Microbiology
Molecular Sequence Data
NUCLEOTIDE
nucleotide sequence
NUCLEOTIDOS
PASTEURELLA MULTOCIDA
Pasteurella multocida - enzymology
Pasteurella multocida - genetics
prediction
Sequence Homology, Nucleic Acid
Structure-Activity Relationship
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Summary:The Pasteurella multocida adenylate cyclase gene has been cloned and expressed in Escherichia coli. The primary structure of the protein (838 amino acids) deduced from the corresponding nucleotide sequence was compared with that of E. coli. The two enzymes have similar molecular sizes and, based on sequence conservation at the protein level, are likely to be organized in two functional domains: the amino-terminal catalytic domain and the carboxy-terminal regulatory domain. It was shown that P. multocida adenylate cyclase synthesizes increased levels of cyclic AMP in E. coli strains deficient in the catabolite gene activator protein compared with wild-type strains. This increase does not occur in strains deficient in both the catabolite gene activator protein and enzyme III-glucose, indicating that a protein similar to E. coli enzyme III-glucose is involved in the regulation of P. multocida adenylate cyclase. It also indicates that the underlying process leading to enterobacterial adenylate cyclase activation has been conserved through evolution
ISSN:0021-9193
1098-5530
1067-8832
DOI:10.1128/jb.173.19.6265-6269.1991