Isolation of an active catalytic core of Streptococcus downei MFe28 GTF-I glucosyltransferase

J Bacteriol. 1999 Apr;181(7):2290-2. doi: 10.1128/JB.181.7.2290-2292.1999.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins*
  • Catalysis
  • Catalytic Domain
  • Escherichia coli
  • Gene Expression
  • Glucosyltransferases / genetics*
  • Mutagenesis
  • Proteins / genetics*
  • Streptococcus / enzymology*
  • Streptococcus / genetics

Substances

  • Bacterial Proteins
  • Proteins
  • GTF-I protein, Streptococcus
  • Glucosyltransferases
  • glucosyltransferase I