TY - JOUR
T1 - N-Terminal 112 amino acid residues are not required for the sialyltransferase activity of Photobacterium damsela α2,6- sialyltransferase
AU - Sun, Mingchi
AU - Li, Yanhong
AU - Chokhawala, Harshal A.
AU - Henning, Ryan
AU - Chen, Xi
PY - 2008/4
Y1 - 2008/4
N2 - 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.
AB - 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.
KW - Carbohydrate
KW - Expression
KW - Photobacterium damsela
KW - Sialic acid
KW - Sialyltransferase
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U2 - 10.1007/s10529-007-9588-y
DO - 10.1007/s10529-007-9588-y
M3 - Article
C2 - 17989925
AN - SCOPUS:43149109297
VL - 30
SP - 671
EP - 676
JO - Biotechnology Letters
JF - Biotechnology Letters
SN - 0141-5492
IS - 4
ER -