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 › peer-review

29 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

Keywords

Carbohydrate
Expression
Photobacterium damsela
Sialic acid
Sialyltransferase

ASJC Scopus subject areas

Biotechnology
Applied Microbiology and Biotechnology
Microbiology
Bioengineering

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@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

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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 -