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 Citations (Scopus)

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

Photobacterium
Sialyltransferases
Amino acids
Proteins
Amino Acids
Ethylenediaminetetraacetic acid
Metal ions
Assays
Fusion reactions
Dithiothreitol
Edetic Acid
Metals
Ions

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 journalArticle

Sun, Mingchi ; Li, Yanhong ; Chokhawala, Harshal A. ; Henning, Ryan ; Chen, Xi. / N-Terminal 112 amino acid residues are not required for the sialyltransferase activity of Photobacterium damsela α2,6- sialyltransferase. In: Biotechnology Letters. 2008 ; Vol. 30, No. 4. pp. 671-676.
@article{f90a73cdafc54cfd9d25bcd0919e408a,
title = "N-Terminal 112 amino acid residues are not required for the sialyltransferase activity of Photobacterium damsela α2,6- sialyltransferase",
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.",
keywords = "Carbohydrate, Expression, Photobacterium damsela, Sialic acid, Sialyltransferase",
author = "Mingchi Sun and Yanhong Li and Chokhawala, {Harshal A.} and Ryan Henning and Xi Chen",
year = "2008",
month = "4",
doi = "10.1007/s10529-007-9588-y",
language = "English (US)",
volume = "30",
pages = "671--676",
journal = "Biotechnology Letters",
issn = "0141-5492",
publisher = "Springer Netherlands",
number = "4",

}

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 -