Evolutionary adaptation of plasmid-encoded enzymes for degrading nylon oligomers

  title={Evolutionary adaptation of plasmid-encoded enzymes for degrading nylon oligomers},
  author={Hirosuke Okada and Seiji Negoro and Hiroyuki Kimura and Shunichi Nakamura},
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… 
The nylon oligomer biodegradation system ofFlavobacterium andPseudomonas
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'.
A plasmid encoding enzymes for nylon oligomer degradation: nucleotide sequence and analysis of pOAD2.
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).
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 of
Amino acid alterations essential for increasing the catalytic activity of the nylon-oligomer-degradation enzyme of Flavobacterium sp.
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.
Plasmid dependence of Pseudomonas sp. strain NK87 enzymes that degrade 6-aminohexanoate-cyclic dimer
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.
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
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.
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 degradation
A new nylon oligomer degradation gene (nylC) on plasmid pOAD2 from a Flavobacterium sp
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.


Plasmid Control of 6-Aminohexanoic Acid Cyclic Dimer Degradation Enzymes of Flavobacterium sp. K172
Results suggested that the genes of the enzymes were borne on pOAD2, which is likely to be derived from pOAD1 by genetic rearrangements such as deletion, insertion, or substitution.
Plasmid-determined enzymatic degradation of nylon oligomers
The nylon oligomer degradation genes on plasmid pOAD2 of Flavobacterium sp.
Purification and characterization of 6-aminohexanoic-acid-oligomer hydrolase of Flavobacterium sp. Ki72.
6-Aminohexanoic-oligomer hydrolase of Flavobacterium sp. KI72 was purified to homogeneity by column chromatography three times, and by preparation polyacrylamide gel electrophoresis twice. The
6-Aminohexanoic acid cyclic dimer hydrolase. A new cyclic amide hydrolase produced by Achromobacter guttatus KI74.
6-Aminohexanoic acid cyclic dimer hydrolase produced by Achromobacter guttatus cells grown on 6-aminohexanoic acid cyclic dimer (1,8-diazacyclotetradecane-2,9-dione) was purified until it was
Molecular basis of altered enzyme specificities in a family of mutant amidases from Pseudomonas aeruginosa.
It is concluded that mutation amiE16 is a Ser leads to Phe change at position 7 from the N-terminus and the effect of this on the enzyme conformation is discussed.
The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites.
  • J. ShineL. Dalgarno
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1974
It is suggested that this region of the RNA is able to interact with mRNA and that the 3'-terminal U-U-A(OH) is involved in the termination of protein synthesis through base-pairing with terminator codons.
The N-terminal amino-acid sequences of DNA polymerase I from Escherichia coli and of the large and the small fragments obtained by a limited proteolysis.
The two fragments obtained by proteolytic cleavage of DNA polymerase I from Escherichia coli have been isolated by chromatography on hydroxyapatite and shows unambiguously that the small fragment is placed in the N-terminal end of the native enzyme.
Construction of plasmids carrying the cI gene of bacteriophage lambda.
By techniques of recombination in vitro, a plasmid bearing the repressor gene (cI) of bacteriophage lambda fused to the promoter of the lac operon is constructed.