UDP‐L‐arabinose‐hydroxyproline‐O‐glycosyltransferases in Volvox carteri

FEBS Letters

Jaenicke, Lothar¹  Günther, Roland¹  Bause, Ernst¹ 

[1] Institut für Biochemie, Zülpicherstrasse 47,5000 Köln 1, FRG

关键词: Hydroxyproline cluster;    O-Arabinosylation;    UDP-L-arabinose-hydroxyproline-O-glycosyltransferase;    (Volvox carteri);    TFA;    trifluoroacetic acid;    Hyp;    hydroxyproline;    Mops;    3-(N-morpholino)propanesulfonic acid;    Boc-;    t-butoxycarbonyl-;    Xaa;    ‘variable’ amino acid;   

DOI  :  10.1016/0014-5793(87)80943-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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).

【 授权许可】

Unknown