Sequence analysis of the Streptococcus mutans scrB gene.
AUTOR(ES)
Sato, Y
RESUMO
The complete nucleotide sequence of the Streptococcus mutans GS-5 scrB gene coding for sucrose-6-phosphate hydrolase activity was determined. A potential ribosome-binding site as well as promoter sequences were identified upstream from the gene. The deduced amino acid sequence of the enzyme suggested a molecular weight of 51,750, which is similar to that estimated for the enzyme isolated from strain GS-5. The enzyme is slightly acidic, with a pI of 5.9, and is a relatively hydrophilic protein. The nucleotide and amino acid sequences of the enzyme showed significant homology with those of the sacA protein from Bacillus subtilis. In addition, a region of amino acid homology with the S. mutans fructosyltransferase and B. subtilis levansucrase proteins was also detected.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=259507Documentos Relacionados
- Sequence analysis of scrA and scrB from Streptococcus sobrinus 6715.
- Genetic analysis of scrA and scrB from Streptococcus sobrinus 6715.
- Molecular cloning and characterization of scrB, the structural gene for the Streptococcus mutans phosphoenolpyruvate-dependent sucrose phosphotransferase system sucrose-6-phosphate hydrolase.
- Sequence analysis of the gtfB gene from Streptococcus mutans.
- Characterization of the major promoter for the plasmid-encoded sucrose genes scrY, scrA, and scrB.