Thiamine diphosphate Dependent Enzymes Engineering Database (TEED) version12.1
part of the BioCatNet
This Internet database integrates information on sequence, structure and function of thiamine dependent enzymes.
The BioCatNet Database System aims to collect and present comprehensive information about biocatalysts: sequence, structure, educts, products, environmental conditions and kinetics. Moreover, it will reveal structure-function relationships to boost development of novel biocatalysts.
To contribute to BioCatNet by submission of functional information, please refer to the information in the BioCatNet Wiki.
The TEED combines sequence, structure and function information on ThDP-dependent enzymes. Thus, it allows for the systematic analysis of this vast and diverse protein family and serves as a comprehensive navigation tool. By enrichment with additional information on the composition of the sequences and structures, the underlying family classification and linked taxonomic information, the TEED forms the most comprehensive repository of this protein family.
Buchholz P. C. F., Vogel C., Reusch W., Pohl M., Rother D., Spieß A. & Pleiss J. (2016). BioCatNet: a database system for the integration of enzyme sequences and biocatalytic experiments. ChemBioChem, 17, 2093-2098.
Vogel C. & Pleiss J. (2014). The modular structure of ThDP-dependent enzymes. Proteins: Structure, Function, and Bioinformatics, 82, 10: 2523-2537.
Hailes H.C., Rother D., Müller M., Westphal R., Ward J.M., Pleiss J., Vogel C. & Pohl M. (2013). Engineering stereoselectivity of ThDP-dependent enzymes. FEBS J 280: 6374 -6394
Vogel C., Widmann M., Pohl M. & Pleiss J. (2012). A standard numbering scheme for thiamine diphosphate-dependent decarboxylases. BMC Biochemistry, 13, 24.
Widmann M., Radloff R. & Pleiss J. (2010). The Thiamine diphosphate dependent Enzyme Engineering Database: A tool for the systematic analysis of sequence and structure relations. BMC Biochemistry, 11, 9.
Knoll M., Müller M., Pleiss J. & Pohl M. (2006). Factors mediating activity, selectivity, andsubstrate specificity for the thiamindiphosphate-dependent enzymesbenzaldehyde lyase and benzoylformatedecarboxylase. Chembiochem 7: 1928-1934