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  • 2000-2004  (4)
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Material
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Year
  • 1
    Electronic Resource
    Electronic Resource
    DIVERGENT EVOLUTION OF ENZYMATIC FUNCTION: Mechanistically Diverse Superfamilies and Functionally Distinct Suprafamilies (2001)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biochemistry 70 (2001), S. 209-246 
    Details
    ISSN: 0066-4154
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Chemistry and Pharmacology , Biology
    Notes: Abstract The protein sequence and structure databases are now sufficiently representative that strategies nature uses to evolve new catalytic functions can be identified. Groups of divergently related enzymes whose members catalyze different reactions but share a common partial reaction, intermediate, or transition state (mechanistically diverse superfamilies) have been discovered, including the enolase, amidohydrolase, thiyl radical, crotonase, vicinal-oxygen-chelate, and Fe-dependent oxidase superfamilies. Other groups of divergently related enzymes whose members catalyze different overall reactions that do not share a common mechanistic strategy (functionally distinct suprafamilies) have also been identified: (a) functionally distinct suprafamilies whose members catalyze successive transformations in the tryptophan and histidine biosynthetic pathways and (b) functionally distinct suprafamilies whose members catalyze different reactions in different metabolic pathways. An understanding of the structural bases for the catalytic diversity observed in super- and suprafamilies may provide the basis for discovering the functions of proteins and enzymes in new genomes as well as provide guidance for in vitro evolution/engineering of new enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.biochem.70.1.209
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    “Fishing” for the functional proteome (2002)
    [s.l.] : Nature Publishing Group
    Nature biotechnology 20 (2002), S. 786-787 
    Details
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] A considerable problem in biology is to identify those members of a proteome that participate in specific biological processes, assign a function to each, and devise strategies for their selective modulation. The recent development of activity-based profiling (ABP), in which a chemical ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nbt0802-786
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Barrels in pieces? (2001)
    [s.l.] : Nature America Inc.
    Nature structural biology 8 (2001), S. 5-7 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] An important outcome of postgenomic biology is the potential for elucidating the evolutionary history of contemporary proteins. Understanding Nature's strategies and mechanisms for enzyme evolution may provide insights for the rational design of proteins with novel biological functions. Because ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/83048
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    New wine from old barrels (2000)
    [s.l.] : Nature America Inc.
    Nature structural biology 7 (2000), S. 171-173 
    Details
    ISSN: 1072-8368
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The versatility of the α/β-barrel fold in supporting different enzymatic functions is well known: as many as 10% of the structures of enzymes may have this fold. In the most common example of this type of structure, a β-sheet–loop–α-helix–loop motif is ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/73249
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    Paper (German National Licenses)
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