A multifunctional Pasteurella multocida sialyltransferase: a powerful tool for the synthesis of sialoside libraries.
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 alpha2,3-sialyltransferase (main function), (2) an alpha2,6-sialyltransferase, (3) an alpha2,3-sialidase, and (4) an alpha2,3-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.
Yu
Hai
H
Department of Chemistry, University of California, One Shields Avenue, Davis, California 95616, USA.
Chokhawala
Harshal
H
Karpel
Rebekah
R
Yu
Hui
H
Wu
Bingyuan
B
Zhang
Jianbo
J
Zhang
Yingxin
Y
Jia
Qiang
Q
Chen
Xi
X
D002240:Carbohydrate Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D006027:Glycosides / Q000096:biosynthesis*; D006595:Hexosamines / Q000378:metabolism; D008969:Molecular Sequence Data; D009438:Neuraminic Acids / Q000378:metabolism; D016979:Pasteurella multocida / Q000201:enzymology* / Q000235:genetics; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism; D012799:Sialyltransferases / Q000235:genetics / Q000378:metabolism*
D006027:Glycosides; D006595:Hexosamines; D009438:Neuraminic Acids; D011994:Recombinant Proteins; C008322:mannosamine; D012799:Sialyltransferases