Altering Active-Site Loop Dynamics Enhances Standalone Activity of the Tryptophan Synthase Alpha Subunit Article Swipe
Cristina Duran
,
Thomas Kinateder
,
Caroline Hiefinger
,
Reinhard Sterner
,
Sílvia Osuna
·
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1021/acscatal.4c04587
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1021/acscatal.4c04587
The α-subunit (TrpA) of the allosterically regulated bifunctional tryptophan synthase αββα enzyme catalyzes the retro-aldol cleavage of indole-glycerol phosphate (IGP) to d-glyceraldehyde 3-phosphate (G3P) and indole. The activity of the enzyme is highly dependent on the β-subunit (TrpB), which allosterically regulates and activates TrpA for enhanced function. This contrasts with the homologous BX1 enzyme from Zea mays that can catalyze the same reaction as TrpA without requiring the presence of any additional binding partner. In this study, we computationally evaluated and compared the conformational landscapes of the homologous ZmBX1 and ZmTrpA enzymes. Our results indicate that enhanced TrpA standalone activity requires the modulation of the conformational dynamics of two relevant active-site loops, loop 6 and 2, that need to be synchronized for accessing the catalytically activated closed state for IGP cleavage, as well as open states for favoring indole/G3P release. Taking as inspiration the evolutionary blueprint ZmBX1 and using our developed correlation-based tool shortest path map focused on the rate-determining conformational transition leading to the catalytically activated closed state, we computationally designed a variant named ZmTrpASPM4-L6BX1, which displays a 163-fold improvement in catalytic efficiency for the retro-aldol cleavage of IGP. This study showcases the importance of fine-tuning the conformational dynamics of active-site loops for altering and improving function, especially in those cases in which a conformational change is rate determining.
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- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1021/acscatal.4c04587
- OA Status
- hybrid
- Cited By
- 12
- References
- 33
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4403996570
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Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4403996570Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1021/acscatal.4c04587Digital Object Identifier
- Title
-
Altering Active-Site Loop Dynamics Enhances Standalone Activity of the Tryptophan Synthase Alpha SubunitWork title
- Type
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articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2024Year of publication
- Publication date
-
2024-11-02Full publication date if available
- Authors
-
Cristina Duran, Thomas Kinateder, Caroline Hiefinger, Reinhard Sterner, Sílvia OsunaList of authors in order
- Landing page
-
https://doi.org/10.1021/acscatal.4c04587Publisher landing page
- Open access
-
YesWhether a free full text is available
- OA status
-
hybridOpen access status per OpenAlex
- OA URL
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https://doi.org/10.1021/acscatal.4c04587Direct OA link when available
- Concepts
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Tryptophan synthase, Active site, Protein subunit, ATP synthase, Chemistry, Alpha (finance), Tryptophan, Loop (graph theory), Catalysis, Stereochemistry, Biochemistry, Enzyme, Amino acid, Psychology, Mathematics, Clinical psychology, Combinatorics, Gene, Psychometrics, Construct validityTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
12Total citation count in OpenAlex
- Citations by year (recent)
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2025: 12Per-year citation counts (last 5 years)
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33Number of works referenced by this work
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10Other works algorithmically related by OpenAlex
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