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 language | English (US) |
|---|---|
| Pages (from-to) | 671-676 |
| Number of pages | 6 |
| Journal | Biotechnology Letters |
| Volume | 30 |
| Issue number | 4 |
| DOIs | |
| State | Published - Apr 2008 |
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Keywords
- Carbohydrate
- Expression
- Photobacterium damsela
- Sialic acid
- Sialyltransferase
ASJC Scopus subject areas
- Biotechnology
- Applied Microbiology and Biotechnology
- Microbiology
- Bioengineering
Cite this
N-Terminal 112 amino acid residues are not required for the sialyltransferase activity of Photobacterium damsela α2,6- sialyltransferase. / Sun, Mingchi; Li, Yanhong; Chokhawala, Harshal A.; Henning, Ryan; Chen, Xi.
In: Biotechnology Letters, Vol. 30, No. 4, 04.2008, p. 671-676.Research output: Contribution to journal › Article
}
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
UR - http://www.scopus.com/inward/record.url?scp=43149109297&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=43149109297&partnerID=8YFLogxK
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 -