Rational Design of Activity-Based Retaining β-Exoglucosidase Probes

Kah-Yee Li; Wouter W. Kallemeijn; Jianbing Jiang; Marthe Walvoort; Lianne Willems; Thomas JM Beenakker; Hans Van Den Elst; Gijs Van Der Marel; Jeroen D C Codée; Hans Aerts; Bogdan I. Florea; Rolf G. Boot; Martin Witte; Herman S. Overkleeft

doi:10.1002/9783527687503.ch13

Rational Design of Activity-Based Retaining β-Exoglucosidase Probes

Kah-Yee Li, Wouter W. Kallemeijn, Jianbing Jiang, Marthe Walvoort, Lianne Willems, Thomas JM Beenakker, Hans Van Den Elst, Gijs Van Der Marel, Jeroen D C Codée, Hans Aerts, Bogdan I. Florea, Rolf G. Boot, Martin Witte, Herman S. Overkleeft

Chemistry

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Abstract

Activity-based probes (ABPs) have been developed for numerous serine hydrolases, cysteine proteases, and threonine hydrolases, but less frequently for other enzyme families. This chapter details the successful development and application of a number of activity-based retaining β-exoglucosidase probes. It discusses how, by rational design, suitable ABPs for retaining β-exoglucosidases can be designed. Mutations in the gene encoding glucosidase, beta, acid (GBA) can lead to partial malfunctioning of the enzyme, leading to accumulation of its substrate, glucosylceramide. This is in a nutshell the basis of the lysosomal storage disorder, Gaucher disease. The aziridine-based scaffold holds more promise, and as one can learn from Cazypedia, there are numerous retaining exoglycosidases that follow the general Koshland mechanism and that are, in principle, amenable to ABPP activity-based protein profiling using cyclitol aziridines emulating in configuration and substitution pattern the corresponding substrate glycosides.

Original language	English
Title of host publication	Concepts and Case Studies in Chemical Biology
Publisher	Wiley-Blackwell
Pages	191-206
Number of pages	16
ISBN (Electronic)	9783527687503
ISBN (Print)	9783527336111
DOIs	https://doi.org/10.1002/9783527687503.ch13
Publication status	Published - 6 Oct 2014

Keywords

Activity-based probes (ABPs)
Activity-based retaining β-exoglucosidase probes
Cyclophellitol aziridine
GBA

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10.1002/9783527687503.ch13

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Li, K.-Y., Kallemeijn, W. W., Jiang, J., Walvoort, M., Willems, L., Beenakker, T. JM., Van Den Elst, H., Van Der Marel, G., Codée, J. D. C., Aerts, H., Florea, B. I., Boot, R. G., Witte, M., & Overkleeft, H. S. (2014). Rational Design of Activity-Based Retaining β-Exoglucosidase Probes. In Concepts and Case Studies in Chemical Biology (pp. 191-206). Wiley-Blackwell. https://doi.org/10.1002/9783527687503.ch13

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title = "Rational Design of Activity-Based Retaining β-Exoglucosidase Probes",

abstract = "Activity-based probes (ABPs) have been developed for numerous serine hydrolases, cysteine proteases, and threonine hydrolases, but less frequently for other enzyme families. This chapter details the successful development and application of a number of activity-based retaining β-exoglucosidase probes. It discusses how, by rational design, suitable ABPs for retaining β-exoglucosidases can be designed. Mutations in the gene encoding glucosidase, beta, acid (GBA) can lead to partial malfunctioning of the enzyme, leading to accumulation of its substrate, glucosylceramide. This is in a nutshell the basis of the lysosomal storage disorder, Gaucher disease. The aziridine-based scaffold holds more promise, and as one can learn from Cazypedia, there are numerous retaining exoglycosidases that follow the general Koshland mechanism and that are, in principle, amenable to ABPP activity-based protein profiling using cyclitol aziridines emulating in configuration and substitution pattern the corresponding substrate glycosides.",

keywords = "Activity-based probes (ABPs), Activity-based retaining β-exoglucosidase probes, Cyclophellitol aziridine, GBA",

author = "Kah-Yee Li and Kallemeijn, {Wouter W.} and Jianbing Jiang and Marthe Walvoort and Lianne Willems and Beenakker, {Thomas JM} and {Van Den Elst}, Hans and {Van Der Marel}, Gijs and Cod{\'e}e, {Jeroen D C} and Hans Aerts and Florea, {Bogdan I.} and Boot, {Rolf G.} and Martin Witte and Overkleeft, {Herman S.}",

year = "2014",

month = oct,

day = "6",

doi = "10.1002/9783527687503.ch13",

language = "English",

isbn = "9783527336111",

pages = "191--206",

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publisher = "Wiley-Blackwell",

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Li, K-Y, Kallemeijn, WW, Jiang, J, Walvoort, M, Willems, L, Beenakker, TJM, Van Den Elst, H, Van Der Marel, G, Codée, JDC, Aerts, H, Florea, BI, Boot, RG, Witte, M & Overkleeft, HS 2014, Rational Design of Activity-Based Retaining β-Exoglucosidase Probes. in Concepts and Case Studies in Chemical Biology. Wiley-Blackwell, pp. 191-206. https://doi.org/10.1002/9783527687503.ch13

TY - CHAP

T1 - Rational Design of Activity-Based Retaining β-Exoglucosidase Probes

AU - Li, Kah-Yee

AU - Kallemeijn, Wouter W.

AU - Jiang, Jianbing

AU - Walvoort, Marthe

AU - Willems, Lianne

AU - Beenakker, Thomas JM

AU - Van Den Elst, Hans

AU - Van Der Marel, Gijs

AU - Codée, Jeroen D C

AU - Aerts, Hans

AU - Florea, Bogdan I.

AU - Boot, Rolf G.

AU - Witte, Martin

AU - Overkleeft, Herman S.

PY - 2014/10/6

Y1 - 2014/10/6

N2 - Activity-based probes (ABPs) have been developed for numerous serine hydrolases, cysteine proteases, and threonine hydrolases, but less frequently for other enzyme families. This chapter details the successful development and application of a number of activity-based retaining β-exoglucosidase probes. It discusses how, by rational design, suitable ABPs for retaining β-exoglucosidases can be designed. Mutations in the gene encoding glucosidase, beta, acid (GBA) can lead to partial malfunctioning of the enzyme, leading to accumulation of its substrate, glucosylceramide. This is in a nutshell the basis of the lysosomal storage disorder, Gaucher disease. The aziridine-based scaffold holds more promise, and as one can learn from Cazypedia, there are numerous retaining exoglycosidases that follow the general Koshland mechanism and that are, in principle, amenable to ABPP activity-based protein profiling using cyclitol aziridines emulating in configuration and substitution pattern the corresponding substrate glycosides.

AB - Activity-based probes (ABPs) have been developed for numerous serine hydrolases, cysteine proteases, and threonine hydrolases, but less frequently for other enzyme families. This chapter details the successful development and application of a number of activity-based retaining β-exoglucosidase probes. It discusses how, by rational design, suitable ABPs for retaining β-exoglucosidases can be designed. Mutations in the gene encoding glucosidase, beta, acid (GBA) can lead to partial malfunctioning of the enzyme, leading to accumulation of its substrate, glucosylceramide. This is in a nutshell the basis of the lysosomal storage disorder, Gaucher disease. The aziridine-based scaffold holds more promise, and as one can learn from Cazypedia, there are numerous retaining exoglycosidases that follow the general Koshland mechanism and that are, in principle, amenable to ABPP activity-based protein profiling using cyclitol aziridines emulating in configuration and substitution pattern the corresponding substrate glycosides.

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EP - 206

BT - Concepts and Case Studies in Chemical Biology

PB - Wiley-Blackwell

ER -

Rational Design of Activity-Based Retaining β-Exoglucosidase Probes

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Keywords

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