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Journal Abstract Search

98 related items for PubMed ID: 8515236

  • 1. Characterization of the 6-aminohexanoate-dimer hydrolase from Pseudomonas sp. NK87.
    Kanagawa K, Oishi M, Negoro S, Urabe I, Okada H.
    J Gen Microbiol; 1993 Apr; 139(4):787-95. PubMed ID: 8515236
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  • 2. Plasmid dependence of Pseudomonas sp. strain NK87 enzymes that degrade 6-aminohexanoate-cyclic dimer.
    Kanagawa K, Negoro S, Takada N, Okada H.
    J Bacteriol; 1989 Jun; 171(6):3181-6. PubMed ID: 2722745
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  • 3. Amino acid alterations essential for increasing the catalytic activity of the nylon-oligomer-degradation enzyme of Flavobacterium sp.
    Kato K, Fujiyama K, Hatanaka HS, Priyambada ID, Negoro S, Urabe I, Okada H.
    Eur J Biochem; 1991 Aug 15; 200(1):165-9. PubMed ID: 1879421
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  • 6. Biodegradation of nylon oligomers.
    Negoro S.
    Appl Microbiol Biotechnol; 2000 Oct 15; 54(4):461-6. PubMed ID: 11092619
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  • 7. Evolutionary adaptation of plasmid-encoded enzymes for degrading nylon oligomers.
    Okada H, Negoro S, Kimura H, Nakamura S.
    Nature; 2000 Oct 15; 306(5939):203-6. PubMed ID: 6646204
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  • 8. The nylon oligomer biodegradation system of Flavobacterium and Pseudomonas.
    Negoro S, Kato K, Fujiyama K, Okada H.
    Biodegradation; 1994 Dec 15; 5(3-4):185-94. PubMed ID: 7765832
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  • 9. X-ray crystallographic analysis of 6-aminohexanoate-dimer hydrolase: molecular basis for the birth of a nylon oligomer-degrading enzyme.
    Negoro S, Ohki T, Shibata N, Mizuno N, Wakitani Y, Tsurukame J, Matsumoto K, Kawamoto I, Takeo M, Higuchi Y.
    J Biol Chem; 2005 Nov 25; 280(47):39644-52. PubMed ID: 16162506
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  • 10. A plasmid encoding enzymes for nylon oligomer degradation: nucleotide sequence and analysis of pOAD2.
    Kato K, Ohtsuki K, Koda Y, Maekawa T, Yomo T, Negoro S, Urabe I.
    Microbiology (Reading); 1995 Oct 25; 141 ( Pt 10)():2585-90. PubMed ID: 7582019
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  • 12. Nylon oligomer degradation gene, nylC, on plasmid pOAD2 from a Flavobacterium strain encodes endo-type 6-aminohexanoate oligomer hydrolase: purification and characterization of the nylC gene product.
    Kakudo S, Negoro S, Urabe I, Okada H.
    Appl Environ Microbiol; 1993 Nov 25; 59(11):3978-80. PubMed ID: 8285701
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  • 14. A novel R-stereoselective amidase from Pseudomonas sp. MCI3434 acting on piperazine-2-tert-butylcarboxamide.
    Komeda H, Harada H, Washika S, Sakamoto T, Ueda M, Asano Y.
    Eur J Biochem; 2004 Apr 25; 271(8):1580-90. PubMed ID: 15066183
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  • 15. A DmpA-homologous protein from Pseudomonas sp. is a dipeptidase specific for beta-alanyl dipeptides.
    Komeda H, Asano Y.
    FEBS J; 2005 Jun 25; 272(12):3075-84. PubMed ID: 15955066
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  • 18. Construction of hybrid genes of 6-aminohexanoic acid-oligomer hydrolase and its analogous enzyme. Estimation of the intramolecular regions important for the enzyme evolution.
    Negoro S, Nakamura S, Kimura H, Fujiyama K, Zhang YZ, Kanzaki N, Okada H.
    J Biol Chem; 1984 Nov 25; 259(22):13648-51. PubMed ID: 6389532
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  • 20. S-stereoselective piperazine-2-tert-butylcarboxamide hydrolase from Pseudomonas azotoformans IAM 1603 is a novel L-amino acid amidase.
    Komeda H, Harada H, Washika S, Sakamoto T, Ueda M, Asano Y.
    Eur J Biochem; 2004 Apr 25; 271(8):1465-75. PubMed ID: 15066172
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