N-terminal 112 amino acid residues are not required for the sialyltransferase activity of Photobacterium damsela α 2,6-sialyltransferase
| Autor: | Ryan Henning, Harshal A. Chokhawala, Xi Chen, Yanhong Li, Mingchi Sun |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2007 |
| Předmět: |
Sialyltransferase
Bioengineering Applied Microbiology and Biotechnology Dithiothreitol Article Chromatography Affinity Residue (chemistry) chemistry.chemical_compound Structure-Activity Relationship Bacterial Proteins Structure–activity relationship Chromatography High Pressure Liquid Edetic Acid Ions biology Chemistry Photobacterium General Medicine biology.organism_classification Fusion protein N-Acetylneuraminic Acid Sialyltransferases Sialic acid Protein Structure Tertiary Enzyme Activation Kinetics Biochemistry biology.protein Electrophoresis Polyacrylamide Gel Protons N-Acetylneuraminic acid Biotechnology |
| Popis: | Photobacterium damsela alpha2,6-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 alpha2,6-sialyltransferase activity. Among four truncated forms tested, N-His-tagged Delta15Pd2,6ST(N) containing 16-497 amino acid residues had the highest expression level. Similar to the Delta15Pd2,6ST(N), the shorter Delta112Pd2,6ST(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. |
| Databáze: | OpenAIRE |
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