Transaldolase: From biochemistry to human disease |
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| Authors: | Anne K Samland Georg A Sprenger |
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| Institution: | 1. Massachusetts General Hospital Cancer Center, Harvard Medical School, Boston, MA 02114, USA;2. Department of Biochemistry and Molecular Genetics, College of Medicine, University of Illinois at Chicago, Chicago, IL 60607, USA;3. Research and Development Section, Jesse Brown VA Medical Center, Chicago, IL 60612, USA;1. Fermentation and Applied Microbiology Laboratory, Department of Chemistry and Life Science, Nihon University, 1866 Kameino, Fujisawa, Kanagawa 252-0880, Japan;2. Biomolecular Engineering Laboratory, National Food Research Institute, 2-1-12, Kannondai, Tsukuba, Ibaraki 305-8642, Japan;3. Systems and Synthetic Biology Program, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, 28049 Madrid, Spain;4. the Escuela de Química, Universidad de Costa Rica, 2060 San José, Costa Rica;5. the Institute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, Switzerland;1. Department of Food Science and Human Nutrition, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA;2. Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA;3. Department of Agricultural Biotechnology and Center for Food and Bioconvergence, Seoul National University, Seoul 151-921, South Korea;4. Department of Chemical & Biological Engineering, Hanbat National University, Daejeon 305-719, South Korea |
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| Abstract: | The role of the enzyme transaldolase (TAL) in central metabolism, its biochemical properties, structure, and role in human disease is reviewed. The nearly ubiquitous enzyme transaldolase is a part of the pentose phosphate pathway and transfers a dihydroxyacetone group from donor compounds (fructose 6-phosphate or sedoheptulose 7-phosphate) to aldehyde acceptor compounds. The phylogeny of transaldolases shows that five subfamilies can be distinguished, three of them with proven TAL enzyme activity, one with unclear function, and the fifth subfamily comprises transaldolase-related enzymes, the recently discovered fructose 6-phosphate aldolases. The three-dimensional structure of a bacterial (Escherichia coli TAL B) and the human enzyme (TALDO1) has been solved. Based on the 3D-structure and mutagenesis studies, the reaction mechanism was deduced. The cofactor-less enzyme proceeds with a Schiff base intermediate (bound dihydroxyacetone). While a transaldolase deficiency is well tolerated in many microorganisms, it leads to severe symptoms in homozygous TAL-deficient human patients. The involvement of TAL in oxidative stress and apoptosis, in multiple sclerosis, and in cancer is discussed. |
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