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Science 13 November 1992:
Vol. 258. no. 5085, pp. 1140 - 1143
DOI: 10.1126/science.1439821
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Articles

Science, Vol 258, Issue 5085, 1140-1143
Copyright © 1992 by American Association for the Advancement of Science

articles

Cooperativity induced by a single mutation at the subunit interface of a dimeric enzyme: glutathione reductase

NS Scrutton, MP Deonarain, A Berry, and RN Perham

Department of Biochemistry, University of Cambridge, United Kingdom.

When glycine418 of Escherichia coli glutathione reductase, which is in a closely packed region of the dimer interface, is replaced with a bulky tryptophan residue, the enzyme becomes highly cooperative (Hill coefficient 1.76) for glutathione binding. The cooperativity is lost when the mutant subunit is hybridized with a wild-type subunit to create a heterodimer. The mutation appears to disrupt atomic packing at the dimer interface, which induces a change of kinetic mechanism. A single mutation in a region of the protein remote from the active site can thus act as a molecular switch to confer cooperativity on an enzyme.


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