Substrate specificity in thiamin diphosphate-dependent decarboxylases |
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| Institution: | 1. Department of Chemistry, Chemistry Research Laboratory, Mansfield Road, Oxford, OX1 3TA, UK;1. Jiangsu Co-Innovation Center of Efficient Processing and Utilization of Forest Resources, Nanjing Forestry University, Nanjing, 210037, People’s Republic of China;2. College of Chemical Engineering, Nanjing Forestry University, Nanjing, 210037, People’s Republic of China;3. Jiangsu Province Key Laboratory of Green Biomass-based Fuels and Chemicals, Nanjing, 210037, People’s Republic of China;1. Department of Biology, University of New Brunswick, Fredericton, NB, Canada E3B 5A3;2. Department of Chemistry, University of Prince Edward Island, Charlottetown, PEI, Canada C1A 4P3;1. University of Zagreb, Faculty of Chemical Engineering and Technology, Savska c. 16, HR-10000 Zagreb, Croatia;2. Institute of Pharmaceutical Sciences, Albert-Ludwigs-Universität Freiburg, Albertstrasse 25, 79104 Freiburg, Germany;1. Structural Biology Unit, Center for Cooperative Research in Biosciences, CIC bioGUNE, 48160 Derio, Spain;2. Department of Biological Sciences, Columbia University, New York, NY 10027, USA;3. Department of Biochemistry and Molecular Biology, University of the Basque Country, P.O. Box 644, 48080 Bilbao, Spain;1. School of Chemistry, University of Manchester, Manchester Institute of Biotechnology, 131 Princess Street, Manchester M1 7DN, UK;2. York Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5DD, UK |
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| Abstract: | Thiamin diphosphate (ThDP) is the biologically active form of vitamin B1, and ThDP-dependent enzymes are found in all forms of life. The catalytic mechanism of this family requires the formation of a common intermediate, the 2α-carbanion–enamine, regardless of whether the enzyme is involved in C–C bond formation or breakdown, or even formation of C?N, C?O and C?S bonds. This demands that the enzymes must screen substrates prior to, and/or after, formation of the common intermediate. This review is focused on the group for which the second step is the protonation of the 2α-carbanion, i.e., the ThDP-dependent decarboxylases. Based on kinetic data, sequence/structure alignments and mutagenesis studies the factors involved in substrate specificity have been identified. |
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