Evolutionary adaptation of plasmid-encoded enzymes for degrading nylon oligomers

@article{Okada1983EvolutionaryAO,
  title={Evolutionary adaptation of plasmid-encoded enzymes for degrading nylon oligomers},
  author={H. Okada and S. Negoro and H. Kimura and Shunichi Nakamura},
  journal={Nature},
  year={1983},
  volume={306},
  pages={203-206}
}
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… Expand
The nylon oligomer biodegradation system ofFlavobacterium andPseudomonas
TLDR
The molecular basis for adaptation of microorganisms toward these xenobiotic compounds, 6-aminohexanoate-oligomer, in Flavobacterium and Pseudomonas strains, is discussed, and the specific activity of the EII enzyme is 200-fold higher than that of EII'. Expand
A plasmid encoding enzymes for nylon oligomer degradation: nucleotide sequence and analysis of pOAD2.
TLDR
Comparison of the sequence of pOAD2 with those in the GenBank and EMBL databases revealed that the deduced amino acid sequences had significant similarity with the sequences of gene products such as oppA-F (oligopeptide permeases), ftsX (filamentation temperature sensitive), penDE (isopenicillin N-acyltransferase) and rep (plasmid incompatibility). Expand
Characterization of the 6-aminohexanoate-dimer hydrolase from Pseudomonas sp. NK87.
The DNA base sequence of the Pseudomonas sp. NK87 gene (P-nylB) for 6-aminohexanoate-dimer hydrolase (P-EII), a xenobiotic-compound-degrading enzyme, was determined. It has an open reading frame ofExpand
Characterization of hybrid enzymes between 6-aminohexanoate-dimer hydrolase and its analogous protein
TLDR
It is demonstrated that EII, EII′, and their hybrid enzymes are highly active only toward the substrates that contain 6-aminohexanoate as the N-terminal residue, while the recognition of the C-Terminal residue in the substrate was not stringent. Expand
Amino acid alterations essential for increasing the catalytic activity of the nylon-oligomer-degradation enzyme of Flavobacterium sp.
TLDR
Construction of various hybrid genes obtained by exchanging fragments flanked by conserved restriction sites of the two genes demonstrated that two amino acid replacements in the EII' enzyme, i.e. Gly181----Asp and His266----Asn, enhanced the activity toward 6-aminohexanoate dimer 1000-fold. Expand
Plasmid dependence of Pseudomonas sp. strain NK87 enzymes that degrade 6-aminohexanoate-cyclic dimer
TLDR
Restriction endonuclease analyses show that the NK87 strain harbors at least six plasmids ranging in size from 20 to 80 kilobase pairs (kbp), and results indicate that the P-EI gene and P- EII gene are encoded on the 23-kbp and 80- kbp plasmid, respectively. Expand
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
TLDR
This study cloned the two genes, nylD1 and nylE1, responsible for 6-aminohexanoate metabolism on the basis of the draft genomic DNA sequence of strain KI72, and amplified the DNA fragments that encode these genes by polymerase chain reaction using a synthetic primer DNA homologous to the 4-aminobutyrate metabolic enzymes. Expand
Characterization of endo-type 6-aminohexanoate-oligomer hydrolase from Flavobacterium sp.
Abstract Cyclic oligomers of 6-aminohexanoate were fractionated from waste materials obtained from a nylon-6 factory by Sephadex LH-20 gel filtration column chromatography, and two major fractions, aExpand
High homology between 6-aminohexanoate-cyclic-dimer hydrolases of Flavobacterium and Pseudomonas strains
The nucleotide sequences of the genes for 6-aminohexanoate-cyclic-dimer hydrolases of Flavobacterium sp. strain K172 (F-nylA) and Pseudomonas sp. NK87 (P-nylA), enzymes essential for the degradationExpand
A new nylon oligomer degradation gene (nylC) on plasmid pOAD2 from a Flavobacterium sp
TLDR
This new Nom1 degrading enzyme (EIII, the nylC gene product) hydrolyzed not only Nom1 but also the N-carbobenzoxy-6-aminohexanoate trimer, a substrate which was not Hydrolyzed by either EI or EII. Expand
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