Structural insights into the half-of-sites reactivity in homodimeric and homotetrameric metalloenzymes |
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| Affiliation: | 1. Department of Chemistry, Georgia State University, Atlanta, GA 30303, USA;2. Department of Chemistry and Center for Diagnostics and Therapeutics, Georgia State University, Atlanta, GA 30303, USA;1. Program in Chemical Biology, University of Massachusetts Chan Medical School, 364 Plantation Street, Worcester, MA 01605, USA;2. Department of Biochemistry and Molecular Biotechnology, University of Massachusetts Chan Medical School, 364 Plantation Street, Worcester, MA 01605, USA;3. From the Department of Medical Biochemistry and Biophysics, Umeå University, SE-901 87 Umeå and;4. the Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden;1. Department of Biology, Technion-Israel Institute of Technology, Haifa 3200003, Israel;2. Centre for Structural Systems Biology (CSSB) and Deutsches Elektronen-Synchrotron DESY, Hamburg, Germany;3. Universitätsklinikum Hamburg-Eppendorf (UKE), Hamburg, Germany;4. European Molecular Biology Laboratory (EMBL), Hamburg, Germany |
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| Abstract: | Half-of-sites reactivity in many homodimeric and homotetrameric metalloenzymes has been known for half a century, yet its benefit remains poorly understood. A recently reported cryo-electron microscopy structure has given some clues on the less optimized reactivity of Escherichia coli ribonucleotide reductase with an asymmetric association of α2β2 subunits during catalysis. Moreover, nonequivalence of enzyme active sites has been reported in many other enzymes, possibly as a means of regulation. They are often induced by substrate binding or caused by a critical component introduced from a neighboring subunit in response to substrate loadings, such as in prostaglandin endoperoxide H synthase, cytidine triphosphate synthase, glyoxalase, tryptophan dioxygenase, and several decarboxylases or dehydrogenases. Overall, half-of-sites reactivity is likely not an act of wasting resources but rather a method devised in nature to accommodate catalytic or regulatory needs. |
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| Keywords: | Enzyme regulation Half-sites reactivity Protein structure–function relationship Allosterism Cooperativity Metalloproteins |
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