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

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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.

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Acknowledgements

This work was supported by NIH R01GM076360 and the start-up funds from the Regents of the University of California.

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Authors and Affiliations

  1. Department of Chemistry, University of California, One Shields Avenue, Davis, CA, 95616, USA

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

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  1. Mingchi Sun
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  2. Yanhong Li
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  3. Harshal A. Chokhawala
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  4. Ryan Henning
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  5. Xi Chen
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Correspondence to Xi Chen.

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Mingchi Sun and Yanhong Li contributed equally to this work.

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Sun, M., Li, Y., Chokhawala, H.A. et al. N-Terminal 112 amino acid residues are not required for the sialyltransferase activity of Photobacterium damsela α2,6-sialyltransferase. Biotechnol Lett 30, 671–676 (2008). https://doi.org/10.1007/s10529-007-9588-y

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  • DOI: https://doi.org/10.1007/s10529-007-9588-y

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