Structural characterization of ligand binding and pH-specific enzymatic activity of mouse Acidic Mammalian Chitinase Article Swipe
Roberto Efraín Díaz
,
Andrew K. Ecker
,
G.J. Correy
,
Pooja Asthana
,
I.D. Young
,
Bryan Faust
,
Michael C. Thompson
,
Ian B. Seiple
,
Steven J. Van Dyken
,
Richard M. Locksley
,
James S. Fraser
·
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.7554/elife.89918.2
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.7554/elife.89918.2
Chitin is an abundant biopolymer and pathogen-associated molecular pattern that stimulates a host innate immune response. Mammals express chitin-binding and chitin-degrading proteins to remove chitin from the body. One of these proteins, Acidic Mammalian Chitinase (AMCase), is an enzyme known for its ability to function under acidic conditions in the stomach but is also active in tissues with more neutral pHs, such as the lung. Here, we used a combination of biochemical, structural, and computational modeling approaches to examine how the mouse homolog (mAMCase) can act in both acidic and neutral environments. We measured kinetic properties of mAMCase activity across a broad pH range, quantifying its unusual dual activity optima at pH 2 and 7. We also solved high resolution crystal structures of mAMCase in complex with oligomeric GlcNAcn, the building block of chitin, where we identified extensive conformational ligand heterogeneity. Leveraging these data, we conducted molecular dynamics simulations that suggest how a key catalytic residue could be protonated via distinct mechanisms in each of the two environmental pH ranges. These results integrate structural, biochemical, and computational approaches to deliver a more complete understanding of the catalytic mechanism governing mAMCase activity at different pH. Engineering proteins with tunable pH optima may provide new opportunities to develop improved enzyme variants, including AMCase, for therapeutic purposes in chitin degradation.
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Metadata
- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.7554/elife.89918.2
- OA Status
- gold
- References
- 54
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4399074834
All OpenAlex metadata
Raw OpenAlex JSON
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https://openalex.org/W4399074834Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.7554/elife.89918.2Digital Object Identifier
- Title
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Structural characterization of ligand binding and pH-specific enzymatic activity of mouse Acidic Mammalian ChitinaseWork title
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preprintOpenAlex work type
- Language
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enPrimary language
- Publication year
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2024Year of publication
- Publication date
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2024-05-28Full publication date if available
- Authors
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Roberto Efraín Díaz, Andrew K. Ecker, G.J. Correy, Pooja Asthana, I.D. Young, Bryan Faust, Michael C. Thompson, Ian B. Seiple, Steven J. Van Dyken, Richard M. Locksley, James S. FraserList of authors in order
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https://doi.org/10.7554/elife.89918.2Publisher landing page
- Open access
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YesWhether a free full text is available
- OA status
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goldOpen access status per OpenAlex
- OA URL
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https://doi.org/10.7554/elife.89918.2Direct OA link when available
- Concepts
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Chitinase, Enzyme, Chemistry, Ligand (biochemistry), Biochemistry, Characterization (materials science), Receptor, Materials science, NanotechnologyTop concepts (fields/topics) attached by OpenAlex
- Cited by
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0Total citation count in OpenAlex
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54Number of works referenced by this work
- Related works (count)
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10Other works algorithmically related by OpenAlex
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| publication_date | 2024-05-28 |
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| referenced_works | https://openalex.org/W1520063126, https://openalex.org/W2194964976, https://openalex.org/W2055280186, https://openalex.org/W2594616832, https://openalex.org/W2606047052, https://openalex.org/W2809920457, https://openalex.org/W1989344768, https://openalex.org/W2072705074, https://openalex.org/W2025131995, https://openalex.org/W1987250042, https://openalex.org/W1983790404, https://openalex.org/W2159764647, https://openalex.org/W2082582948, https://openalex.org/W2090919511, https://openalex.org/W2141218426, https://openalex.org/W2085791010, https://openalex.org/W2057381625, https://openalex.org/W2106083621, https://openalex.org/W2055968806, https://openalex.org/W2043583435, https://openalex.org/W3000284194, https://openalex.org/W2166434234, https://openalex.org/W2749441863, https://openalex.org/W1935712031, https://openalex.org/W2087082796, https://openalex.org/W2035160545, https://openalex.org/W1974515964, https://openalex.org/W3202137709, https://openalex.org/W2889895086, https://openalex.org/W2098303032, https://openalex.org/W2105732409, https://openalex.org/W2070695325, https://openalex.org/W2120641909, https://openalex.org/W2108307958, https://openalex.org/W3155165073, https://openalex.org/W2160907977, https://openalex.org/W2330799739, https://openalex.org/W2590248011, https://openalex.org/W2981206605, https://openalex.org/W1985352887, https://openalex.org/W4200614587, https://openalex.org/W2529584704, https://openalex.org/W1895968703, https://openalex.org/W2003176514, https://openalex.org/W2031468563, https://openalex.org/W2793311671, https://openalex.org/W2108921801, https://openalex.org/W2163341755, https://openalex.org/W2154197653, https://openalex.org/W2144081223, https://openalex.org/W2557476528, https://openalex.org/W2731784911, https://openalex.org/W2113904137, https://openalex.org/W3125756628 |
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