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On the conservation of protein sequences in evolution
Authors:Kisters-Woike B  Vangierdegom C  Müller-Hill B
Affiliation:1. Medical Research Council Centre for Regenerative Medicine, University of Edinburgh, 5 Little France Drive, Edinburgh, Scotland EH16 4UU, UK;2. Centre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK;3. Leibniz Institute for Natural Product Research and Infection Biology eV-Hans-Knoll Institute, Jena, Germany;4. National Institute for Biological Standards and Control (MHRA), Blanche Lane, South Mimms, Hertfordshire EN6 3QG, UK;5. IfADo-Leibniz Research Centre for Working Environment and Human Factors at the Technical University Dortmund, Dortmund, Germany;1. Wayne State University School of Medicine, Detroit Medical Center, 4707 St Antoine Street, Detroit, MI 48201, USA;2. Chicago Medical School at Rosalind Franklin University, 3333 Greenbay Road, North Chicago, IL 60064, USA;3. Department of Orthopaedic Surgery, Detroit Medical Center, 4201 St Antoine Street, Suite 9B, Detroit, MI 48201, USA;4. Resident Research Partnership, 233 Fielding Street, Suite B, Ferndale, MI 48220, USA;1. Department of Pharmacokinetics, Biochemistry and Metabolism, Chiesi Farmaceutici S.p.A, 43122 Parma, Italy;2. Laboratory of Cellular Therapy, Division of Oncology, Department of Medical and Surgical Sciences for Children and Adults, University Hospital of Modena and Reggio Emilia, Modena, Italy
Abstract:The amino acid sequences of enzymes like alcohol dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase are strongly conserved across all phyla. We suggest that the amino acid conservation of such enzymes might be a result of the fact that they function as part of a multi-enzyme complex. The specific interactions between the proteins involved would hinder evolutionary change of their surfaces.
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