In 2010 the first recombinant pathway to enable biologcal production of alkanes was discovered. Connecting the key enzyme for alkane production, aldehyde deformylating oxygenase (ADO, Figure 1), to alternative biosynthetic pathways can enable biological production of propane (i.e. natural gas), octane (i.e. gasoline), tetradecane (i.e. jet fuel), heptadecane (i.e. diesel), and numerous other petrochemicals. To achieve this vision we need to expand on recent efforts in this area, which have often found ADO activity and specificity as limiting. Therefore, we propose develop a deeper understanding of the ADO structure-function relationship in order to rationally modulate activity and specificity. In turn this will enable the development of ADO enzymes and synthetic pathways capable of producing each of the products mentioned in a complex cellular environment.<br/><br/>We have recently made a significant discovery of over 30 enzymes diverse in sequence capable of catalyzing the ADO reaction. This is a transformative expansion for this class of soluble enzymes, and is providing unique insight into the structural determinants that are critical for ADO functionality. Until now this reaction has been thought of as a unique function from several cyanobacteria, and all known enzymes with ADO activity were highly homologous in sequence. Due to the high homology the identification unique and conserved features that enable ADO function has been difficult. However, many of the new enzymes we discovered share less than 20% sequence identity to any previously known enzyme capable of catalyzing this important reaction, with some as low as 5%. Many of these new enzymes are from organisms outside the cyanobacteria phylum (e.g. Nitrospirae, Firmicutes, or Actinobacteria) and even the bacterial kingdom (e.g. Archea Crenarchaeota). In order to take full advantage of this discovery it is critical to structurally and kinetically characterize these enzymes. This will provide unprecedented insight into the structural determinants of ADO activity and specificity, enabling the design of novel ADO enzymes for the biological production of fuels and industrially important chemicals.

Exploring the functional landscape of aldehyde deformylating oxygenase activity throughout the ferritin superfamily

253rd National Meeting (2017)

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