NDLI: Human lysosomal α-mannosidases exhibit different inhibition and metal binding properties

Content Provider	PubMed Central
Author	Venkatesan, Meenakshi Kuntz, Douglas A. Rose, David R.
Abstract	Two structurally-related members of the lysosomal mannosidase family, the broad substrate specificity enzyme human lysosomal α-mannosidase (hLM, MAN2B1) and the human core α-1, 6-specific mannosidase (hEpman, MAN2B2) act in a complementary fashion on different glycosidic linkages, to effect glycan degradation in the lysosome. We have successfully expressed these enzymes in Drosophila S2 cells and functionally characterized them. hLM and hEpman were significantly inhibited by the class II α-mannosidase inhibitors, swainsonine and mannostatin A. We show that three pyrrolidine-based compounds designed for selective inhibition of Golgi α-mannosidase II (GMII) exhibited varying degrees of inhibition for hLM and hEpman. While these compounds inhibited hLM and GMII similarly, they inhibited hEpman to a lesser extent. Further, the two lysosomal α-mannosidases also show differential metal dependency properties. This has led us to propose a secondary metal binding site in hEpman. These results set the stage for the development of selective inhibitors to members of the GH38 family, and, henceforth, the further investigation of their physiological roles.
Related Links	http://dx.doi.org/10.1002/pro.235
Ending Page	2251
Page Count	10
Starting Page	2242
File Format	PDF
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science : A Publication of the Protein Society
Issue Number	11
Volume Number	18
Language	English
Publisher	Wiley Subscription Services, Inc., A Wiley Company
Publisher Date	2009-11-01
Access Restriction	Open
Rights Holder	Wiley Subscription Services, Inc., A Wiley Company
Subject Keyword	Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Human lysosomal alpha-mannosidases exhibit different inhibition and metal binding properties.

Intracellular transport of human lysosomal α-mannosidase and α-mannosidosis-related mutants

Structure-activity relationship of swainsonine. Inhibition of human alpha-mannosidases by swainsonine analogues.

Family 47 α-Mannosidases in N-Glycan Processing

The structural basis of the inhibition of human alpha-mannosidases by azafuranose analogues of mannose.

‘Click chemistry‘ synthesis of 1-(α-d-mannopyranosyl)-1,2,3-triazoles for inhibition of α-mannosidases

Human lysosomal elastase. Catalytic and immunological properties.

Inhibition of N-linked oligosaccharide trimming mannosidases blocks human B cell development.

Mechanistic insights into a Ca2+-dependent family of α-mannosidases in a human gut symbiont

Human lysosomal α-mannosidases exhibit different inhibition and metal binding properties

Similar Documents

Human lysosomal alpha-mannosidases exhibit different inhibition and metal binding properties.

Intracellular transport of human lysosomal α-mannosidase and α-mannosidosis-related mutants

Structure-activity relationship of swainsonine. Inhibition of human alpha-mannosidases by swainsonine analogues.

Family 47 α-Mannosidases in N-Glycan Processing

The structural basis of the inhibition of human alpha-mannosidases by azafuranose analogues of mannose.

‘Click chemistry‘ synthesis of 1-(α-d-mannopyranosyl)-1,2,3-triazoles for inhibition of α-mannosidases

Human lysosomal elastase. Catalytic and immunological properties.

Inhibition of N-linked oligosaccharide trimming mannosidases blocks human B cell development.

Mechanistic insights into a Ca2+-dependent family of α-mannosidases in a human gut symbiont

Human lysosomal α-mannosidases exhibit different inhibition and metal binding properties