Together with our team of scientists, you will identify new or novel enzyme candidates for your reaction or process based on the structural features of active sites. To identify these enzymes, we use in-silico methods using our CatalophoreTM platform, a combination of prepared protein structural data (CATALObase), and search algorithms and patterns tailored to your specific needs.
The application of our CatalophoreTM technology for industrial biotechnology enables, among other things:
– the catalysis of novel biochemical reactions (e.g., proteins with altered substrate specificity and selectivity),
– the engineering/optimization of existing protein properties (e.g., activity, stability, robustness),
– the extension of freedom to operate (FTO) by identifying and developing alternative proteins, or
– the acceleration and improvement of improving established optimization strategies employing engineering.
– strengthen your patent
– the acceleration and improvement of existing engineering optimization strategies
Get in touch with our team of scientists for help with projects related to structural bioinformatics, such as homology modeling (automated modeling for large datasets is also available), substrate docking (single or automated docking using our cavity-guided docking approach), or molecular-dynamics (MD) simulations.
Upon request, our cooperation partners can provide you with biochemical expertise for follow-up wet-lab projects and work packages.
Even though our platforms are ready-to-use, we do not believe in one-fits-all solutions. Tailor-made software solutions help you optimize your R&D pipeline and redefine how you solve problems. Our developers are committed to eliminating bottlenecks and adapting our CatalophoreTM platform to your needs. Our AI-driven technologies learn and grow with your projects and are customizable to your goals.
Back in 2014, we demonstrated the power of 3D point clouds in enzyme search. Instead of sequence searches, finding a similar cavity led to a surprising result.
Read more here: Steinkellner, C. C. Gruber, T. Pavkov-Keller, A. Binter, K. Steiner, C. Winkler, A. Lyskowski, O. Schwamberger, M. Oberer, H. Schwab, K. Faber, P. Macheroux, K. Gruber, Nat. Commun. 2014, 5, 4150.