Year: 1988
Type: article
Abstract: 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.
Source: Infection and Immunity
Authors: Y Sato, H K Kuramitsu
Institution: Northwestern University
Language: English
Subfield: Genetics
Domain: Life Sciences
Open Access status: bronze
Award: G673371051
OpenAlex ID: W2146428713