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Technology Available for Licensing Atomic resolution protein structures as guide for directed engineering of 1,3-butadiene producing enzyme linalool dehydratase/isomerase Max-Planck-Innovation GmbH Amalienstr. 33 80799 Munich Germany File no.: MI-2021-4945-MG Phone: +49 (89) 29 09 19 - 0 Fax: +49 (89) 29 09 19 - 99 [email protected] www.max-planck-innovation.de Contact: Dr. Mareike Göritz Tel.: +49 89 290919-32 [email protected] Background Butadiene is a central intermediate in the manufacture of polymers and synthetic rubbers with a global production volume of 13 million metric tons by 2020. Conventionally, butadiene is produced by classical chemical processes such as steam cracking or dehydrogenation of aliphatic alcohols. These methods rely on petroleum-derived feed stocks. To overcome future obstacles due to the increasing demand of butadiene and decreasing petroleum resources, biobased production is expected to emerge within the next 10 years. Due to its enzymatic activity to convert small organic substrate molecules into butadiene, the recently described Linalool dehydratase/isomerase (Ldi)1 has the potential to become a central biotechnological tool that enables efficient petroleum-independent production of butadiene. Thus there is an urgent need for atomic resolution structural information that are crucial to elucidate the catalytic mechanism of Ldi and to adapt the enzyme to industrial needs. In addition stable, crystal-grade protein for subsequent biochemical and of biophysical characterization is needed to evaluate engineered Ldi derivatives. Technology Researches of the Max Planck Institutes of Marine Microbiology and Biophysics solved two high-resolution crystal structures of Ldi, in the apo- and the ligand-bound state. These structures reveal for the first time the three-dimensional architecture of Ldi, an enzyme that does not share any sequence similarity with any other previously described protein. Furthermore the location of the ligand binding site was unambiguously assigned and the mode of binding and catalysis could be resolved at atomic resolution. To obtain protein crystals diffracting to high resolution, an optimized purification protocol was developed that delivers homogenous, monodisperse and stable crystal-grade protein. Taken together the solved crystal structures together with the developed purification protocol will provide valuable tools for the optimization of Ldi for the biotechnological production of butadiene. Licensing this know-how will provide you with a head-start in this emerging field. Literature 1. Brodkorb, D. et al., Journal of Biological Chemistry, 2010