Flavobacterium sp. KI72 metabolizes 6-aminohexanoic acid cyclic dimer, a by-product of nylon manufacture1, through two newly evolved enzymes, 6-aminohexanoic acid cyclic dimer hydrolase (EI)2 and 6-aminohexanoic acid linear oligomer hydrolase (EII)3. These enzymes are active towards man-made compounds, the cyclic dimer and linear oligomers of 6-aminohexanoic acid respectively, but not towards any of the natural amide bonds tested2,3. The structural genes of EI (nylA) and EII (nylB) are encoded on pOAD2, one of three plasmids harboured in Flavobacterium sp. KI724,5. This plasmid contains two kinds of repeated sequence (RS-I and RS-II); one of the two RS-II sequences, RS-IIA, contains the nylB gene6, while the other, RS-IIB, contains a homologous nylB′ gene. From comparisons of the nucleotide sequences and gene products of the nylB and nylB′ genes, we now conclude that EII enzyme is newly evolved by gene duplication followed by base substitutions on the same plasmid.
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Okada, H., Negoro, S., Kimura, H. et al. Evolutionary adaptation of plasmid-encoded enzymes for degrading nylon oligomers. Nature 306, 203–206 (1983). https://doi.org/10.1038/306203a0
Metabolic pathway of 6-aminohexanoate in the nylon oligomer-degrading bacterium Arthrobacter sp. KI72: identification of the enzymes responsible for the conversion of 6-aminohexanoate to adipate
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