Structural Basis for Catalysis and Inhibition ofN-Glycan Processing Class I α1,2-Mannosidases

Vallée, François; Karaveg, Khanita; Herscovics, Annette; Moremen, Kelley W.; Howell, P. Lynne

doi:10.1074/jbc.m006927200

Cited by 156Glycosylation and Glycoproteins ResearchEnzyme Structure and FunctionEndoplasmic Reticulum Stress and Disease

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Structural Basis for Catalysis and Inhibition ofN-Glycan Processing Class I α1,2-Mannosidases

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Vallée, François, Karaveg, Khanita, Herscovics, Annette, Moremen, Kelley W., Howell, P. Lynne·2000·Journal of Biological Chemistry

DOI 10.1074/jbc.m006927200

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Abstract

Endoplasmic reticulum (ER) class I alpha1,2-mannosidase (also known as ER alpha-mannosidase I) is a critical enzyme in the maturation of N-linked oligosaccharides and ER-associated degradation. Trimming of a single mannose residue acts as a signal to target misfolded glycoproteins for degradation by the proteasome. Crystal structures of the catalytic domain of human ER class I alpha1,2-mannosidase have been determined both in the presence and absence of the potent inhibitors kifunensine and 1-deoxymannojirimycin. Both inhibitors bind to the protein at the bottom of the active-site cavity, with the essential calcium ion coordinating the O-2' and O-3' hydroxyls and stabilizing the six-membered rings of both inhibitors in a (1)C(4) conformation. This is the first direct evidence of the role of the calcium ion. The lack of major conformational changes upon inhibitor binding and structural comparisons with the yeast alpha1, 2-mannosidase enzyme-product complex suggest that this class of inverting enzymes has a novel catalytic mechanism. The structures also provide insight into the specificity of this class of enzymes and provide a blueprint for the future design of novel inhibitors that prevent degradation of misfolded proteins in genetic diseases.

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“Some iminosugars such as swainsonine [263], deoxymannojirimycin [264], castanospermine [265] have proved to be good inhibitors.”
Background
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Crystal structure of a class I α1,2‐mannosidase involved in N‐glycan processing and endoplasmic reticulum quality control
Vallée, F., Lipari, F., Yip, P., Sleno, B., Herscovics, A. A., & Howell, P. L. (2000) · The EMBO Journal · doi:10.1093/emboj/19.4.581 · Cited by 101
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Structure of Penicillium citrinum α1,2-Mannosidase Reveals the Basis for Differences in Specificity of the Endoplasmic Reticulum and Golgi Class I Enzymes
Lobsanov, Y. D., Vallée, F., Imberty, A., Yoshida, T., Yip, P., Herscovics, A. A., & Howell, P. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110243200 · Cited by 49
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Comparison of Kifunensine and 1-Deoxymannojirimycin Binding to Class I and II α-Mannosidases Demonstrates Different Saccharide Distortions in Inverting and Retaining Catalytic Mechanisms,
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Structure of Mouse Golgi α-Mannosidase IA Reveals the Molecular Basis for Substrate Specificity among Class 1 (Family 47 Glycosylhydrolase) α1,2-Mannosidases
Tempel, W., Karaveg, K., Liu, Z., Rose, J. P., Wang, B., & Moremen, K. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403065200 · Cited by 58
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Mechanism of Class 1 (Glycosylhydrolase Family 47) α-Mannosidases Involved in N-Glycan Processing and Endoplasmic Reticulum Quality Control
Karaveg, K., Siriwardena, A. H., Tempel, W., Liu, Z., Glushka, J., Wang, B., & Moremen, K. W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500119200 · Cited by 116
Self-citation

Authors: Vallée, F., Karaveg, K., Herscovics, A., Moremen, K. W., & Howell, P. L.
Affiliations: Hospital for Sick Children (CA)
University of Georgia (US)
McGill University (CA)
University of Toronto (CA)
Corresponding author: Howell, P. Lynne
ORCID: Vallée, François
Moremen, Kelley W.
Howell, P. Lynne
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2000-12
Volume: 275
Issue: 52
Pages: 41287-41298
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m006927200
OpenAlex: W2071513798
Cited by: 152
References: 74
Citations by year: 2026: 1 · 2025: 5 · 2024: 3 · 2023: 4 · 2022: 3 · 2021: 6 · 2020: 8 · 2019: 4 · 2018: 4 · 2017: 5 · 2016: 6 · 2015: 6 · 2014: 4 · 2013: 5 · 2012: 9
FWCI: 2.17
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7248 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institute of General Medical Sciences (GM 31265, R01GM031265, GM-47533, R01GM047533)
National Center for Research Resources (RR 05351)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Keywords: N-glycan processing, kifunensine, 1-deoxymannojirimycin, calcium ion coordination, enzyme-inhibitor complex, ER-associated degradation, misfolded protein degradation, enzyme specificity, crystal structure
MeSH terms: Alkaloids, Amino Acid Sequence, Animals, Calcium, Catalysis, Endoplasmic Reticulum, Humans, Mannosidases, Molecular Sequence Data, Polysaccharides, Protein Conformation, Rabbits, Recombinant Proteins, Structure-Activity Relationship, 1-Deoxynojirimycin

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Structural Basis for Catalysis and Inhibition ofN-Glycan Processing Class I α1,2-Mannosidases

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