A single Glu-to-Lys substitution leads to the loss of the β-diox
enzymatic activity. The three different mutations found in the β-diox
cDNA encoded by the ninaBP315 allele were
introduced separately in the wild-type cDNA by site-directed
mutagenesis, and the resultant plasmids were tested for enzymatic
activity in the E. coli test system. Only the mutation
at position 838 leading to a Glu-to-Lys exchange in the deduced amino
acid sequence results in a loss of β-diox enzymatic activity, whereas
the mutations at positions 1,411 and 1,430 do not affect the enzymatic
activity of β-diox. By converting the mutation at position 838 in the
ninaBP315 cDNA, the enzymatic activity of
the encoded protein could be restored.