Inhibition and Crystal Structure of the Human DHTKD1-Thiamin Diphosphate Complex Article Swipe
João Leandro
,
Susmita Khamrui
,
Hui Wang
,
Chalada Suebsuwong
,
Natalia S. Nemeria
,
Khoi Huynh
,
Moses Moustakim
,
Cody Secor
,
May D. Wang
,
Tetyana Dodatko
,
Brandon Stauffer
,
Christopher G. Wilson
,
Chunli Yu
,
Michelle R. Arkin
,
Frank Jordan
,
Roberto Sánchez
,
Robert J. DeVita
,
Michael B. Lazarus
,
Sander M. Houten
·
YOU?
·
· 2020
· Open Access
·
· DOI: https://doi.org/10.1101/2020.01.20.913012
YOU?
·
· 2020
· Open Access
·
· DOI: https://doi.org/10.1101/2020.01.20.913012
DHTKD1 is the E1 component of the 2-oxoadipic acid dehydrogenase complex (OADHc), which functions in the L-lysine degradation pathway. Mutations in DHTKD1 have been associated with 2-aminoadipic and 2-oxoadipic aciduria, Charcot-Marie-Tooth disease type 2Q (CMT2Q) and eosinophilic esophagitis (EoE). A crystal structure and inhibitors of DHTKD1 could improve the understanding of these clinically distinct disorders, but are currently not available. Here we report the identification of adipoylphosphonic acid and tenatoprazole as DHTKD1 inhibitors using targeted and high throughput screening, respectively. We furthermore elucidate the DHTKD1 crystal structure with thiamin diphosphate bound at 2.1 Å. The protein assembles as a dimer with residues from both monomers contributing to cofactor binding. We also report the impact of ten DHTKD1 missense mutations on the encoded proteins by enzyme kinetics, thermal stability and structural modeling. Some DHTKD1 variants displayed impaired folding (S777P and S862I), whereas other substitutions rendered the enzyme inactive (L234G, R715C and R455Q) or affected the thermal stability and catalytic efficiency (V360A and P773L). Three variants (R163Q, Q305H and G729R) surprisingly showed wild type like properties. Our work provides a structural basis for further understanding of the function of DHTKD1 and a starting point for selective small molecule inhibitors of the enzyme, which could help tease apart the role of this enzyme in several human pathologies.
Related Topics
Concepts
Enzyme
Biochemistry
Chemistry
Cofactor
Missense mutation
Protein structure
Transferase
Biology
Mutation
Gene
Metadata
- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.1101/2020.01.20.913012
- https://www.biorxiv.org/content/biorxiv/early/2020/01/21/2020.01.20.913012.full.pdf
- OA Status
- green
- Cited By
- 2
- References
- 55
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W3002383060
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W3002383060Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1101/2020.01.20.913012Digital Object Identifier
- Title
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Inhibition and Crystal Structure of the Human DHTKD1-Thiamin Diphosphate ComplexWork title
- Type
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preprintOpenAlex work type
- Language
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enPrimary language
- Publication year
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2020Year of publication
- Publication date
-
2020-01-21Full publication date if available
- Authors
-
João Leandro, Susmita Khamrui, Hui Wang, Chalada Suebsuwong, Natalia S. Nemeria, Khoi Huynh, Moses Moustakim, Cody Secor, May D. Wang, Tetyana Dodatko, Brandon Stauffer, Christopher G. Wilson, Chunli Yu, Michelle R. Arkin, Frank Jordan, Roberto Sánchez, Robert J. DeVita, Michael B. Lazarus, Sander M. HoutenList of authors in order
- Landing page
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https://doi.org/10.1101/2020.01.20.913012Publisher landing page
- PDF URL
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https://www.biorxiv.org/content/biorxiv/early/2020/01/21/2020.01.20.913012.full.pdfDirect link to full text PDF
- Open access
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YesWhether a free full text is available
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greenOpen access status per OpenAlex
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https://www.biorxiv.org/content/biorxiv/early/2020/01/21/2020.01.20.913012.full.pdfDirect OA link when available
- Concepts
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Enzyme, Biochemistry, Chemistry, Cofactor, Missense mutation, Protein structure, Transferase, Biology, Mutation, GeneTop concepts (fields/topics) attached by OpenAlex
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2Total citation count in OpenAlex
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2023: 1, 2020: 1Per-year citation counts (last 5 years)
- References (count)
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55Number of works referenced by this work
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10Other works algorithmically related by OpenAlex
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| referenced_works | https://openalex.org/W1999351218, https://openalex.org/W2025032853, https://openalex.org/W1993086445, https://openalex.org/W2774380138, https://openalex.org/W2800875425, https://openalex.org/W2111760474, https://openalex.org/W2065070435, https://openalex.org/W2945611017, https://openalex.org/W775830568, https://openalex.org/W2801479130, https://openalex.org/W2034939856, https://openalex.org/W2754226141, https://openalex.org/W1967314244, https://openalex.org/W2334114285, https://openalex.org/W2081505294, https://openalex.org/W2094767163, https://openalex.org/W2157935454, https://openalex.org/W4248083976, https://openalex.org/W2153819784, https://openalex.org/W2038599206, https://openalex.org/W1994120446, https://openalex.org/W2619776529, https://openalex.org/W2046064201, https://openalex.org/W2562460119, https://openalex.org/W1986745697, https://openalex.org/W2092963470, https://openalex.org/W1999090137, https://openalex.org/W2035503835, https://openalex.org/W2160185798, https://openalex.org/W2091160232, https://openalex.org/W2972971354, https://openalex.org/W4293247451, https://openalex.org/W1981117090, https://openalex.org/W2404333324, https://openalex.org/W2084195157, https://openalex.org/W2917868259, https://openalex.org/W2606318152, https://openalex.org/W1991001144, https://openalex.org/W2162424885, https://openalex.org/W2039067501, https://openalex.org/W1963829486, https://openalex.org/W2143660875, https://openalex.org/W2110808180, https://openalex.org/W2163341755, https://openalex.org/W2094646744, https://openalex.org/W2127130852, https://openalex.org/W2180229411, https://openalex.org/W2162244749, https://openalex.org/W2067921100, https://openalex.org/W2124026197, https://openalex.org/W2098167941, https://openalex.org/W2800016335, https://openalex.org/W2128635872, https://openalex.org/W1563650227, https://openalex.org/W255996521 |
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| corresponding_author_ids | https://openalex.org/A5050646319, https://openalex.org/A5027726446 |
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