[HTML][HTML] Regulation of a cytosolic and nuclear O-GlcNAc transferase: role of the tetratricopeptide repeats
LK Kreppel, GW Hart - Journal of Biological Chemistry, 1999 - ASBMB
The O-GlcNAc transferase (OGT) is a unique nuclear and cytosolic glycosyltransferase that
contains multiple tetratricopeptide repeats. We have begun to characterize the mechanisms
regulating OGT using a combination of deletion analysis and kinetic studies. Here we show
that the p110 subunit of the enzyme forms both homo-and heterotrimers that appear to have
different binding affinities for UDP-GlcNAc. The multimerization domain of OGT lies within
the tetratricopeptide repeat domain and is not necessary for activity. Kinetic analyses of the …
contains multiple tetratricopeptide repeats. We have begun to characterize the mechanisms
regulating OGT using a combination of deletion analysis and kinetic studies. Here we show
that the p110 subunit of the enzyme forms both homo-and heterotrimers that appear to have
different binding affinities for UDP-GlcNAc. The multimerization domain of OGT lies within
the tetratricopeptide repeat domain and is not necessary for activity. Kinetic analyses of the …