Allosteric enzymes as models for chemomechanical energy transducing assemblies
Abstract
In chemomechanical energy transducing assemblies such as muscle and ATP synthase, substrates and macromolecules are locked together as partners where energy available from (or required for) a chemical transformation is exchanged with protein conformational changes. Allosteric binding proteins and enzymes are also chemomechanical energy transducers, using binding energy to generate protein conformational changes, and transduce energy in amounts almost as large as those used to drive muscle contraction and the synthesis of ATP. The recently determined structure of the F1‐ATPase reveals a direct correspondence between the types of conformational changes in this transducer and simpler allosteric binding proteins and enzymes. Therefore, we can examine the structural and energetic data available on allosteric proteins to understand the linkage between ligand binding and global conformational changes in more complex energy transducing assemblies.—Goldsmith, E. J. Allosteric enzymes as models for chemomechanical energy transducing assemblies. FASEB J . 10, 702‐708 (1996)
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JNK and p38 may act as chemomechanical energy transducers, using peptide binding energy to generate allosteric conformational changes.
“This implies that JNK and p38 may act as chemomechanical energy transducers, using peptide binding energy to generate allosteric conformational changes (Goldsmith, 1996).”
From Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125 (2004) · cites this paper as Goldsmith, 1996
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- Authors
- Goldsmith, E. J.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- Corresponding author
- Goldsmith, Elizabeth J.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 1996-05
- Volume
- 10
- Issue
- 7
- Pages
- 702-708
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W1595850413
- Cited by
- 25
- References
- 0
- Citations by year
- 2024: 1 · 2018: 1 · 2013: 2
- FWCI
- 0.88
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The FASEB Journal (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- allosteric enzymes, protein conformational change, F1-ATPase, ligand binding, muscle contraction, ATP synthase, binding energy
- MeSH terms
- Adenosine Triphosphate, Allosteric Regulation, Animals, Catalysis, Energy Metabolism, Proton-Translocating ATPases, Protein Conformation
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