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  • 1
    Electronic Resource
    Electronic Resource
    Microbial metabolism of d- and l-phenylglycine by Pseudomonas putida LW-4 (1986)
    Springer
    Archives of microbiology 144 (1986), S. 169-174 
    Details
    ISSN: 1432-072X
    Keywords: Phenylglycine degradation ; Transamination of d- and l-phenylglycine ; Pseudomonas putida
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A strain of Pseudomonas putida capable of utilizing both stereoisomers of phenylglycine as the sole carbon and energy source was isolated from soil. No phenylglycine racemase was detected in cells grown on either stereoisomer. In an initial reaction each steroisomer of phenylglycine was transaminated yielding phenylglyoxylate which was further metabolized via benzaldehyde to benzoate. Subsequently, benzoate was further degraded via an ortho-cleavage of catechol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414730
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Isolation and characterization of alkene-utilizing Xanthobacter spp. (1986)
    Springer
    Archives of microbiology 145 (1986), S. 403-407 
    Details
    ISSN: 1432-072X
    Keywords: Propene ; 1-Butene ; Xanthobacter ; Mono-oxygenase ; Nitrogen fixation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Yellow-pigmented bacteria showing typical characteristics of Xanthobacter spp. were isolated from enrichments with propene and 1-butene, using classical techniques. The generation time for growth on propene and 1-butene of these bacteria ranged from 5 to 7h. A NADH-dependent mono-oxygenase was identified in cell-free extract of Xanthobacter Py2. This mono-oxygenase was not influenced by potential inhibitors tested indicating that propene mono-oxygenase is different from other hydrocarbon mono-oxygenases described until now. Nitrogenase activity could be measured using the acetylene reduction assay with propene as energy source, because acetylene did not inhibit the mono-oxygenase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00470879
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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