YqhD: a broad-substrate range aldehyde reductase with various applications in production of biorenewable fuels and chemicals |
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Authors: | Laura R Jarboe |
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Institution: | (1) Department of Chemical and Biological Engineering, Iowa State University, Ames, IA 50011, USA |
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Abstract: | The Escherichia coli NADPH-dependent aldehyde reductase YqhD has contributed to a variety of metabolic engineering projects for production of
biorenewable fuels and chemicals. As a scavenger of toxic aldehydes produced by lipid peroxidation, YqhD has reductase activity
for a broad range of short-chain aldehydes, including butyraldehyde, glyceraldehyde, malondialdehyde, isobutyraldehyde, methylglyoxal,
propanealdehyde, acrolein, furfural, glyoxal, 3-hydroxypropionaldehyde, glycolaldehyde, acetaldehyde, and acetol. This reductase
activity has proven useful for the production of biorenewable fuels and chemicals, such as isobutanol and 1,3- and 1,2-propanediol;
additional capability exists for production of 1-butanol, 1-propanol, and allyl alcohol. A drawback of this reductase activity
is the diversion of valuable NADPH away from biosynthesis. This YqhD-mediated NADPH depletion provides sufficient burden to
contribute to growth inhibition by furfural and 5-hydroxymethyl furfural, inhibitory contaminants of biomass hydrolysate.
The structure of YqhD has been characterized, with identification of a Zn atom in the active site. Directed engineering efforts
have improved utilization of 3-hydroxypropionaldehyde and NADPH. Most recently, two independent projects have demonstrated
regulation of yqhD by YqhC, where YqhC appears to function as an aldehyde sensor. |
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