N-Terminal 112 amino acid residues are not required for the sialyltransferase activity of Photobacterium damsela α2,6- sialyltransferase

Mingchi Sun, Yanhong Li, Harshal A. Chokhawala, Ryan Henning, Xi Chen

Research output: Contribution to journalArticle

28 Scopus citations

Abstract

Photobacterium damsela α2,6-sialyltransferase was cloned as N- and C- His-tagged fusion proteins with different lengths (16-497 aa or 113-497 aa). Expression and activity assays indicated that the N-terminal 112 amino acid residues of the protein were not required for its α2,6-sialyltransferase activity. Among four truncated forms tested, N-His-tagged Δ15Pd2,6ST(N) containing 16-497 amino acid residues had the highest expression level. Similar to the Δ15Pd2,6ST(N), the shorter Δ112Pd2,6ST(N) was active in a wide pH range of 7.5-10.0. A divalent metal ion was not required for the sialyltransferase activity, and the addition of EDTA and dithiothreitol did not affect the activity significantly.

Original languageEnglish (US)
Pages (from-to)671-676
Number of pages6
JournalBiotechnology Letters
Volume30
Issue number4
DOIs
StatePublished - Apr 2008

    Fingerprint

Keywords

  • Carbohydrate
  • Expression
  • Photobacterium damsela
  • Sialic acid
  • Sialyltransferase

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Microbiology
  • Bioengineering

Cite this