Fusing catalase to an alkane-producing enzyme maintains enzymatic activity by converting the inhibitory byproduct H2O2 to the cosubstrate O2.

@article{Andre2013FusingCT,
  title={Fusing catalase to an alkane-producing enzyme maintains enzymatic activity by converting the inhibitory byproduct H2O2 to the cosubstrate O2.},
  author={Carl Andre and Sung Won Kim and Xiao-Hong Yu and John Shanklin},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2013},
  volume={110 8},
  pages={3191-6}
}
Biologically produced alkanes represent potential renewable alternatives to petroleum-derived chemicals. A cyanobacterial pathway consisting of acyl-Acyl Carrier Protein reductase and an aldehyde-deformylating oxygenase (ADO) converts acyl-Acyl Carrier Proteins into corresponding n-1 alkanes via aldehyde intermediates in an oxygen-dependent manner (K(m) for O(2), 84 ± 9 µM). In vitro, ADO turned over only three times, but addition of more ADO to exhausted assays resulted in additional product… CONTINUE READING
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