Dominik Hege, Yvonne Gemmecker, Iris Schall, Paula Oppong-Nti, Georg Schmitt, Johann Heider
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引用次数: 0
Abstract
The NAD+-dependent aldehyde dehydrogenase AldB from Aromatoleum aromaticum was recombinantly produced in Escherichia coli and biochemically characterized. As suggested by its substrate spectrum, the most probably physiological function of AldB is the oxidation of short aliphatic aldehydes such as acetaldehyde, which occur as intermediates in the degradation of the corresponding alcohols. In addition, we generated some mutant variants in residue Tyr460, which is located at the neck region of the substrate channel and analyzed their effects on the catalytic parameters for different substrates. Single amino acid exchanges at this position revealed profound changes in substrate preference and substrate inhibition of the variants.
• Small aliphatic aldehydes show the best catalytic efficiency with aldehyde dehydrogenase AldB
• Amino acid exchanges at Y460 results in changed catalytic efficiencies and substrate inhibition
• AldB is a member of a new clade of the aldehyde dehydrogenase superfamily
期刊介绍:
Applied Microbiology and Biotechnology focusses on prokaryotic or eukaryotic cells, relevant enzymes and proteins; applied genetics and molecular biotechnology; genomics and proteomics; applied microbial and cell physiology; environmental biotechnology; process and products and more. The journal welcomes full-length papers and mini-reviews of new and emerging products, processes and technologies.