title: Substrate specificity of hydrolase activity of the primer-dependent glucosyltransferases from Streptococcus sobrinus.
abstract: Four kinds of glucosyltransferases, P1, P2, P3 and P4, were separately purified from the culture supernatant of Streptococcus sobrinus. Their dependencies on primer were analysed. There were two primer-dependent glucosyltransferases (P3 and P4). In the absence of primer 1,6-alpha-D-glucan, P3 was not able to produce glucan from sucrose. However, P3 showed sucrose hydrolase activity, whereas P4 was still able to produce glucan without primer 1,6-alpha-D-glucan. Consequently, glucosyltransferase activity of P4 was incompletely primer-dependent. Both P3 and P4 showed high substrate specificity for sucrose, failing to use melezitose, raffinose, or stachyose as the substrates.
authors.affiliation: Department of Preventive Dentistry, Kyushu Dental College, Kitakyushu, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Hanada
authors.forename: T
authors.initials: T
authors.lastname: Takehara
mesh_terms: D002851:Chromatography, High Pressure Liquid; D005936:Glucans / Q000378:metabolism; D005964:Glucosyltransferases / Q000378:metabolism*; D006836:Hydro-Lyases / Q000378:metabolism*; D013291:Streptococcus / Q000201:enzymology*; D013379:Substrate Specificity; D013395:Sucrose / Q000378:metabolism
chemical_list: D005936:Glucans; D013395:Sucrose; D005964:Glucosyltransferases; D006836:Hydro-Lyases