Title : The hexopyranosyl
residue that is C-glycosidically linked to the side chain of
tryptophan-7 in human
RNase Us is alpha-mannopyranose
Abstract :
- Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530]
- Identification of this monosaccharide is a prerequisite for studies of its biosynthesis and its biological relevance
- Using vicinal proton-proton coupling constants and rotating-frame nuclear Overhauser enhancements, ewe demonstrate that the C-linked substituent is alpha-mannopyranose
- Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale
Output (sent_index, trigger,
protein,
sugar,
site):
- 4. glycopeptide, , -, -, glycopeptide
- 4. moiety, , -, a glycopeptide, glycopeptide
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):