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  • Methylobacterium sp.  (1)
  • Proteins  (1)
  • methylotrophic bacteria  (1)
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  • 1
    ISSN: 1572-9729
    Schlagwort(e): Dichloromethane ; dichloromethane dehalogenase ; glutathione S-transferase ; methylotrophic bacteria ; Methylobacterium sp. ; Methylophilus sp.
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Energietechnik , Land- und Forstwirtschaft, Gartenbau, Fischereiwirtschaft, Hauswirtschaft
    Notizen: Abstract Dichloromethane (DCM) is efficiently utilized as a carbon and energy source by aerobic, Gram-negative, facultative methylotrophic bacteria. It also serves as a sole carbon and energy source for a nitrate-respiringHyphomicrobium sp. and for a strictly anaerobic co-culture of a DCM-fermenting bacterium and an acetogen. The first step of DCM utilization by methylotrophs is catalyzed by DCM dehalogenase which, in a glutathione-dependent substitution reaction, forms inorganic chloride and S-chloromethyl glutathione. This unstable intermediate decomposes to glutathione, inorganic chloride and formaldehyde, a central metabolite of methylotrophic growth. Genetic studies on DCM utilization are beginning to shed some light on questions pertaining to the evolution of DCM dehalogenases and on the regulation of DCM dehalogenase expression. DCM dehalogenase belongs to the glutathione S-transferase supergene family. Analysis of the amino acid sequences of two bacterial DCM dehalogenases reveals 56% identity, and comparison of these sequences to those of glutathione S-transferases indicates a closer relationship to class Theta eukaryotic glutathione S-transferases than to a number of bacterial glutathione S-transferases whose sequences have recently become available.dcmA, the structural gene of the highly substrate-inducible DCM dehalogenase, is carried in most DCM utilizing methylotrophs on large plasmids. InMethylobacterium sp. DM4 its expression is governed bydcmR, a regulatory gene located upstream ofdcmA. dcmR encodes atrans-acting factor which negatively controls DCM dehalogenase formation at the transcriptional level. Our working model thus assumes that thedcmR product is a repressor which, in the absence of DCM, binds to the promoter region ofdcmA and thereby inhibits initiation of transcription.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 28 (1989), S. 535-554 
    ISSN: 0570-0833
    Schlagwort(e): Protein design ; Proteins ; Template synthesis ; Chemistry ; General Chemistry
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: Advances in methodology in both chemistry and molecular biology allow us to take a fresh look at protein science. Chemical synthesis of peptides and site-directed mutagenesis are now standard research tools, paving the way for the construction of new proteins with tailor-made structural and functional properties. The decisive hurdle on the way lies not in the synthesis of the molecules proper but rather in a better understanding of the complex folding pathways of polypeptide chains into spatially well-defined structures. Can the chemist use his synthetic tools to bypass the notorious “folding problem?” In this article, we present a new approach developed in our laboratory, which opens a chemical route to artificial proteins with predetermined three-dimensional structures, allowing a first step towards the synthesis of new proteins with functional properties.
    Zusätzliches Material: 24 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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