A multifunctional Pasteurella multocida sialyltransferase: A powerful tool for the synthesis of sialoside libraries

Hai Yu, Harshal Chokhawala, Rebekah Karpel, Hui Yu, Bingyuan Wu, Jianbo Zhang, Yingxin Zhang, Qiang Jia, Xi Chen

Research output: Contribution to journalArticle

219 Citations (Scopus)

Abstract

A multifunctional sialyltransferase has been cloned from Pasteurella multocida strain P-1059 and expressed in E. coli as a truncated C-terminal His6-tagged recombinant protein (tPm0188Ph). Biochemical studies indicate that the obtained protein is (1) an α2,3-sialyltransferase (main function), (2) an α2,6-sialyltransferase, (3) an α2,3-sialidase, and (4) an α2,3-trans-sialidase. The recombinant tPm0188Ph is a powerful tool in the synthesis of structurally diverse sialoside libraries due to its relaxed substrate specificity, high solubility, high expression level, and multifunctionality.

Original languageEnglish (US)
Pages (from-to)17618-17619
Number of pages2
JournalJournal of the American Chemical Society
Volume127
Issue number50
DOIs
StatePublished - Dec 21 2005

Fingerprint

Sialyltransferases
Pasteurella multocida
Recombinant proteins
Escherichia coli
Libraries
Solubility
Proteins
Substrates
Neuraminidase
Substrate Specificity
Recombinant Proteins

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

A multifunctional Pasteurella multocida sialyltransferase : A powerful tool for the synthesis of sialoside libraries. / Yu, Hai; Chokhawala, Harshal; Karpel, Rebekah; Yu, Hui; Wu, Bingyuan; Zhang, Jianbo; Zhang, Yingxin; Jia, Qiang; Chen, Xi.

In: Journal of the American Chemical Society, Vol. 127, No. 50, 21.12.2005, p. 17618-17619.

Research output: Contribution to journalArticle

Yu, Hai ; Chokhawala, Harshal ; Karpel, Rebekah ; Yu, Hui ; Wu, Bingyuan ; Zhang, Jianbo ; Zhang, Yingxin ; Jia, Qiang ; Chen, Xi. / A multifunctional Pasteurella multocida sialyltransferase : A powerful tool for the synthesis of sialoside libraries. In: Journal of the American Chemical Society. 2005 ; Vol. 127, No. 50. pp. 17618-17619.
@article{c060995d215b4f6cb233194cf32b9ccd,
title = "A multifunctional Pasteurella multocida sialyltransferase: A powerful tool for the synthesis of sialoside libraries",
abstract = "A multifunctional sialyltransferase has been cloned from Pasteurella multocida strain P-1059 and expressed in E. coli as a truncated C-terminal His6-tagged recombinant protein (tPm0188Ph). Biochemical studies indicate that the obtained protein is (1) an α2,3-sialyltransferase (main function), (2) an α2,6-sialyltransferase, (3) an α2,3-sialidase, and (4) an α2,3-trans-sialidase. The recombinant tPm0188Ph is a powerful tool in the synthesis of structurally diverse sialoside libraries due to its relaxed substrate specificity, high solubility, high expression level, and multifunctionality.",
author = "Hai Yu and Harshal Chokhawala and Rebekah Karpel and Hui Yu and Bingyuan Wu and Jianbo Zhang and Yingxin Zhang and Qiang Jia and Xi Chen",
year = "2005",
month = "12",
day = "21",
doi = "10.1021/ja0561690",
language = "English (US)",
volume = "127",
pages = "17618--17619",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "50",

}

TY - JOUR

T1 - A multifunctional Pasteurella multocida sialyltransferase

T2 - A powerful tool for the synthesis of sialoside libraries

AU - Yu, Hai

AU - Chokhawala, Harshal

AU - Karpel, Rebekah

AU - Yu, Hui

AU - Wu, Bingyuan

AU - Zhang, Jianbo

AU - Zhang, Yingxin

AU - Jia, Qiang

AU - Chen, Xi

PY - 2005/12/21

Y1 - 2005/12/21

N2 - A multifunctional sialyltransferase has been cloned from Pasteurella multocida strain P-1059 and expressed in E. coli as a truncated C-terminal His6-tagged recombinant protein (tPm0188Ph). Biochemical studies indicate that the obtained protein is (1) an α2,3-sialyltransferase (main function), (2) an α2,6-sialyltransferase, (3) an α2,3-sialidase, and (4) an α2,3-trans-sialidase. The recombinant tPm0188Ph is a powerful tool in the synthesis of structurally diverse sialoside libraries due to its relaxed substrate specificity, high solubility, high expression level, and multifunctionality.

AB - A multifunctional sialyltransferase has been cloned from Pasteurella multocida strain P-1059 and expressed in E. coli as a truncated C-terminal His6-tagged recombinant protein (tPm0188Ph). Biochemical studies indicate that the obtained protein is (1) an α2,3-sialyltransferase (main function), (2) an α2,6-sialyltransferase, (3) an α2,3-sialidase, and (4) an α2,3-trans-sialidase. The recombinant tPm0188Ph is a powerful tool in the synthesis of structurally diverse sialoside libraries due to its relaxed substrate specificity, high solubility, high expression level, and multifunctionality.

UR - http://www.scopus.com/inward/record.url?scp=29344431622&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=29344431622&partnerID=8YFLogxK

U2 - 10.1021/ja0561690

DO - 10.1021/ja0561690

M3 - Article

C2 - 16351087

AN - SCOPUS:29344431622

VL - 127

SP - 17618

EP - 17619

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 50

ER -