Document Type

Article

Research Focus Area

Biorenewables

Publication Date

2011

Journal or Book Title

Applied Microbiology and Biotechnology

Volume

89

Issue

2

First Page

249

Last Page

257

DOI

10.1007/s00253-010-2912-9

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.

Comments

This is a manuscript of an article from Applied Microbiology and Biotechnology 89 (2010):249, doi: 10.1007/s00253-010-2912-9. Posted with permission. The final publication is available at Springer via http://dx.doi.org/10.1007/s00253-010-2912-9.

Copyright Owner

Springer-Verlag

Language

en

File Format

application/pdf

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