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

doi:10.1007/s10529-007-9588-y

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

Chemistry

Research output: Contribution to journal › Article

28 Scopus citations

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	https://doi.org/10.1007/s10529-007-9588-y
State	Published - Apr 2008

Fingerprint

Keywords

Carbohydrate
Expression
Photobacterium damsela
Sialic acid
Sialyltransferase

ASJC Scopus subject areas

Biotechnology
Applied Microbiology and Biotechnology
Microbiology
Bioengineering

Cite this

Sun, M., Li, Y., Chokhawala, H. A., Henning, R., & Chen, X. (2008). N-Terminal 112 amino acid residues are not required for the sialyltransferase activity of Photobacterium damsela α2,6- sialyltransferase. Biotechnology Letters, 30(4), 671-676. https://doi.org/10.1007/s10529-007-9588-y

@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 = apr

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 -

Access to Document

10.1007/s10529-007-9588-y