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  • 1995-1999  (2)
  • Benzoate 4-hydroxylase  (1)
  • Chemoattractant  (1)
  • 1
    Electronic Resource
    Electronic Resource
    A newly identified chemotactic sexual pheromone from Closterium ehrenbergii (1998)
    Springer
    Sexual plant reproduction 11 (1998), S. 81-85 
    Details
    ISSN: 1432-2145
    Keywords: Key words Closterium ehrenbergii ; Chemoattractant ; Conjugation ; Sexual pheromone ; Protoplast-release-inducing protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  In sexual reproduction of Closterium ehrenbergii, pairing with the sexual partner cells is the first process observed. A cell migration-inducing activity, specific for mating-type plus (mt+; NIES-228) cells, was detected in the culture medium of mating-type minus (mt–; NIES-229) cells. Light was necessary for production of the active substance by mt– cells and for migration of mt+ cells. The active substance was heat-labile and had an apparent molecular mass of 20 kDa, as determined by gel filtration. A protein of 20 kDa was detected in the active fraction of gel filtration after sodium dodecyl sulfate polyacrylamide gel electrophoresis. Based on these results, it is proposed that a chemotactic sexual pheromone involved in the formation of sexual pairs of cells is secreted by mt– cells of C. ehrenbergii and is proteinaceous, like other sexual pheromones secreted by Closterium species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004970050123
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Structural characterization of the gene and corresponding cDNA for the cytochrome P450rm from Rhodotorula minuta which catalyzes formation of isobutene and 4-hydroxylation of benzoate (1997)
    Springer
    Molecular genetics and genomics 256 (1997), S. 115-120 
    Details
    ISSN: 1617-4623
    Keywords: Key wordsRhodotorula minuta ; Cytochrome P450 ; Benzoate 4-hydroxylase ; CYP53B1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cytochrome P450rm was previously isolated from the basidiomycete yeast Rhodotorula minuta as a bifunctional enzyme with isobutene-forming and benzoate 4-hydroxylase activities. We cloned the gene and corresponding cDNA for P450rm in order to characterize the enzyme in the context of fungal phylogeny and physiology. From the cDNA sequence, P450rm was deduced to have 527 amino acids with a calculated molecular weight of 59 136. P450rm shared 48% amino acid sequence identity with CYP53A1 from Aspergillus niger, indicating that the gene belongs to a novel subfamily of CYP53, CYP53B. However, the organization of the P450rm gene, which has eight exons and seven introns, differed completely to that of CYP53A1. Northern analysis demonstrated that the level of P450rm mRNA expression increased when L-phenylalanine was used as sole carbon source. These results suggest that P450rm has been well conserved during the evolution of fungi as a benzoate 4-hydroxylase in the dissimilation pathway starting from L-phenylalanine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050552
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    Paper (German National Licenses)
    Fulltext
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