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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