Isolation of an active catalytic core of Streptococcus downei MFe28 GTF-I glucosyltransferase.
Truncated variants of GTF-I from Streptococcus downei MFe28 were purified by means of a histidine tag. Sequential deletions showed that the C-terminal domain was not directly involved in the catalytic process but was required for primer activation. A fully active catalytic core of only 100 kDa was isolated.
Monchois
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Department of Oral Biology, The Dental School, University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4BW, United Kingdom. vincent.monchois@ncl.ac.uk
Arguello-Morales
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Russell
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D001426:Bacterial Proteins; D002384:Catalysis; D020134:Catalytic Domain; D004926:Escherichia coli; D015870:Gene Expression; D005964:Glucosyltransferases / Q000235:genetics*; D016296:Mutagenesis; D011506:Proteins / Q000235:genetics*; D013291:Streptococcus / Q000201:enzymology* / Q000235:genetics
D001426:Bacterial Proteins; D011506:Proteins; C067118:GTF-I protein, Streptococcus; D005964:Glucosyltransferases; C489364:glucosyltransferase I