Premium
UDP‐L‐arabinose‐hydroxyproline‐ O ‐glycosyltransferases in Volvox carteri
Author(s) -
Günther Roland,
Bause Ernst,
Jaenicke Lothar
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80943-2
Subject(s) - chemistry , arabinose , biochemistry , trifluoroacetic acid , stereochemistry , chromatography , fermentation , xylose
Hydroxyproline‐containing peptides of different length and amino acid sequence have been used to demonstrate UDP‐L‐arabinose‐hydroxyproline‐ O ‐glycosyltransferases in a crude microsomal fraction from the green alga Volvox carteri . The formation of O ‐glycosidic linkages by transfer of UDP‐activated arabinose to the side chain of hydroxyproline was concluded from the resistance of the glycopeptides under the basic conditions of β‐elimination and their susceptibility to hydrolysis by trifluoroacetic acid. This treatment yielded arabinose as the only cleavage product. Arabinose transfer to the various peptide substrates was found to be stimulated by low concentrations of detergent, to require divalent cations and to proceed optimally at pH values around 7.0. The smallest arabinose acceptor peptide was the tripeptide Tyr‐Hyp‐Lys. The glycosyl acceptor electivity increased with increasing numbers of repeated hydroxyproline residues, suggesting that hydroxyproline clusters critically affect substrate recognition by the Volvox transferase(s).