Zobrazeno 1 - 10
of 12
pro vyhledávání: '"A E Kuhm"'
Publikováno v:
International Journal of Systematic and Evolutionary Microbiology. 55:1077-1081
The taxonomic position of a Pseudomonas-like strain, designated BN9T, was investigated. This strain had previously been isolated as a 5-aminosalicylate-degrading organism from a 6-aminonaphthalene-2-sulphonate-degrading mixed bacterial culture. Previ
Autor:
Christa Lechner, Thomas Storm, Andreas Stolz, Thorsten Reemtsma, Jan-Peter Hintner, Ulrich Riegert, A E Kuhm
Publikováno v:
Journal of Bacteriology. 183:6936-6942
In cell extracts of Pseudaminobacter salicylatoxidans strain BN12, an enzymatic activity was detected which converted salicylate in an oxygen-dependent but NAD(P)H-independent reaction to a product with an absorbance maximum at 283 nm. This metabolit
Publikováno v:
Archives of Microbiology. 161:320-327
The range of substituted naphthalenesulfonates which are metabolized by Pseudomonas sp. BN6 were investigated. Resting cells from strain BN6 oxidized 1- and 2-naphthalenesulfonate, 1-hydroxynaphthalene-2-sulfonate, 2,6-naphthalenedisulfonate and all
Publikováno v:
Journal of Biological Chemistry. 268:9484-9489
2'-Hydroxybenzalpyruvate aldolase catalyzes the cleavage of 2'-hydroxybenzalpyruvate to salicylaldehyde and pyruvate. This reaction is part of the degradative pathways for naphthalene and naphthalenesulfonates by bacteria. 2'-Hydroxybenzalpyruvate al
Publikováno v:
Biodegradation. 4:155-162
2-Hydroxychromene-2-carboxylate isomerase activity was found in cell-free systems from bacteria that degrade naphthalenesulfonates. The enzyme fromPseudomonas testosteroni A3 was activated by incubation with glutathione, dithiothreitol or mercaptoeth
Publikováno v:
Archives of Microbiology. 156:218-222
2,4-Dichloro-cis,cis-muconate is established as ringcleavage product in the degradation of 3,5-dichlorocatechol by Alcaligenes eutrophus JMP 134. The formerly described isomerization of 2-chloro-trans- to 2-chlorocis-4-carboxymethylenebut-2-en-4-olid
Publikováno v:
Journal of Bacteriology. 173:3795-3802
1,2-Dihydroxynaphthalene dioxygenase was purified to homogeneity from a bacterium that degrades naphthalenesulfonic acids (strain BN6). The enzyme requires Fe2+ for maximal activity and consists of eight identical subunits with a molecular weight of
Autor:
Feigel B, Matthias Reuss, Manfred Rizzi, H J Knackmuss, Dangmann E, Angela Hammer, A E Kuhm, Naruemol Noisommit-Rizzi, Alexandra Stolz
Publikováno v:
Biodegradation. 7(3)
The mutualistic interactions in a 4-aminobenzenesulfonate (sulfanilate) degrading mixed bacterial culture were studied. This coculture consisted of Hydrogenophaga palleronii strain S1 and Agrobacterium radiobacter strain S2. In this coculture only st
Autor:
A E Kuhm, Josef Altenbuchner, Joachim Klein, Claudia Müller, Alexandra Stolz, Gesche Heiss, H J Knackmuss
Publikováno v:
Journal of bacteriology. 177(20)
An extradiol dioxygenase was cloned from the naphthalenesulfonate-degrading bacterial strain BN6 by screening a gene bank for colonies with 2,3-dihydroxybiphenyl dioxygenase activity. DNA sequence analysis of a 1,358-bp fragment revealed an open read
Publikováno v:
The Journal of biological chemistry. 268(13)
2'-Hydroxybenzalpyruvate aldolase catalyzes the cleavage of 2'-hydroxybenzalpyruvate to salicylaldehyde and pyruvate. This reaction is part of the degradative pathways for naphthalene and naphthalenesulfonates by bacteria. 2'-Hydroxybenzalpyruvate al