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The CBR superfamily is a group of FAD-dependent oxidoreductases catalyzing the reduction of a broad range of carbonyl-containing substrates. Aspergillus fumigatus possesses two genes (afcR1 and afcR2) encoding putative CBR enzymes. The cbrC mutant of A. fumigatus is unable to utilize various common aldehydes as sole carbon sources. To investigate whether the CBR superfamily enzymes would use aldehyde substrates, recombinant AfcR1 and AfcR2 were expressed as a His(6)-tagged protein and purified using Ni-NTA column chromatography. AfcR1 showed high specific activities with acetaldehyde, propionaldehyde and crotonaldehyde at pH 7.0 and 37 degrees C. AfcR2, however, showed a low activity towards these aldehydes. Other substrates, such as the aldehydes, methylglyoxal, and 3-methyl-2-oxobutyrate, commonly found in the cytoplasm, were not reduced by AfcR1 and AfcR2. A cbrC strain of A. fumigatus showed significantly reduced growth on n-propanol and phenyl acetate, whereas the growth of c
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