Hydrophobic Interactions Contribute to Conformational Stabilization of Endoglycoceramidase II by Mechanism-Based Probes-Reference-Cited by-同舟云学术

Hydrophobic Interactions Contribute to Conformational Stabilization of Endoglycoceramidase II by Mechanism-Based Probes

Published:2016-08-16 Issue:34 Volume:55 Page:4823-4835
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Ben Bdira Fredj¹,Jiang Jianbing²,Kallemeijn Wouter³,de Haan Annett⁴,Florea Bogdan I.²,Bleijlevens Boris⁴,Boot Rolf³,Overkleeft Herman S.²,Aerts Johannes M.³,Ubbink Marcellus¹

Affiliation:

1. Department of Macromolecular Biochemistry, Leiden Institute of Chemistry, Einsteinweg 55, 2333 CC Leiden, The Netherlands

2. Department of Bio-organic Synthesis, Leiden Institute of Chemistry, Einsteinweg 55, 2333 CC Leiden, The Netherlands

3. Department of Medical Biochemistry, Leiden Institute of Chemistry, Einsteinweg 55, 2333 CC Leiden, The Netherlands

4. Department of Medical Biochemistry, Academic Medical Center, Meibergdreef 15, 1105 AZ Amsterdam, The Netherlands

Funder

China Scholarship Council

Nederlandse Organisatie voor Wetenschappelijk Onderzoek

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.6b00363

Reference60 articles.

1. A novel glycosphingolipid-degrading enzyme cleaves the linkage between the oligosaccharide and ceramide of neutral and acidic glycosphingolipids.

2. A unique glycosphingolipid-splitting enzyme (ceramide-glycanase from leech) cleaves the linkage between the oligosaccharide and the ceramide

3. Occurrence of ceramide-glycanase in the earthworm, Lumbricusterrestris

4. Hydrophobic nature of mammalian ceramide glycanases: purified from rabbit and rat mammary tissues.

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