Premium
Allosteric enzymes as models for chemomechanical energy transducing assemblies
Author(s) -
Goldsmith Elizabeth J.
Publication year - 1996
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.10.7.8635687
Subject(s) - allosteric regulation , allosteric enzyme , chemistry , biophysics , enzyme , atp synthase , atpase , conformational change , biochemistry , biology
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)