Development and application of a highly α2,6-selective pseudosialidase

31 August 2017, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


In this manuscript we address an important gap in our current carbohydrate active enzyme toolbox, by developing a highly a2,6-selective (over a2,3-selective) de facto sialidase that is necessary both for glycan analysis and glycoconjugate remodeling. Both glycosidic linkages are commonly found in animal biology and each has been shown to have distinct biological function.

Our approach is novel in that it harnesses the high selectivity of known glycosyltransferases ‘in reverse’ for effective hydrolysis, converting transferases to hydrolases by reaction engineering.

More specifically, we demonstrate that the a2,6-specific pseudosialidase activity of Photobacterium sp. JT-ISH-224 a2,6-sialyltransferase can be used effectively for highly a2,6 selective hydrolysis on a broad range of analytes: small synthetic probes, isolated complex glycans and complex mixtures of glycoproteins.


alpha2,6-linkage specificity
glycan analysis

Supplementary materials

Pseudosialidase JACS Supporting Information final


Comments are not moderated before they are posted, but they can be removed by the site moderators if they are found to be in contravention of our Commenting Policy [opens in a new tab] - please read this policy before you post. Comments should be used for scholarly discussion of the content in question. You can find more information about how to use the commenting feature here [opens in a new tab] .
This site is protected by reCAPTCHA and the Google Privacy Policy [opens in a new tab] and Terms of Service [opens in a new tab] apply.