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  • 2000-2004  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    The structure of human liver fructose-1,6-bisphosphate aldolase (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1526-1533 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The X-ray crystallographic structure of the human liver isozyme of fructose-1,6-bisphosphate aldolase has been determined by molecular replacement using a tetramer of the human muscle isozyme as a search model. The liver aldolase (B isozyme) crystallized in space group C2, with unit-cell parameters a = 291.1, b = 489.8, c = 103.4 Å, α = 90, β = 103.6, γ = 90°. These large unit-cell parameters result from the presence of 18 subunits in the asymmetric unit: four catalytic tetramers and a dimer from a fifth tetramer positioned on the twofold crystallographic axis. This structure provides further insight into the factors affecting isozyme specificity. It reveals small differences in secondary structure that occur in regions previously determined to be isozyme specific. Two of these regions are at the solvent-exposed enzyme surface away from the active site of the enzyme. The most significant changes are in the flexible C-terminal region of the enzyme, where there is an insertion of an extra α-helix. Point mutations of the human liver aldolase are responsible for the disease hereditary fructose intolerance. Sequence information is projected onto the new crystal structure in order to indicate how these mutations bring about reduced enzyme activity and affect structural stability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901012719
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  • 2
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray analysis of a γ-lactamase (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 284-286 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: An enzyme from Comomonas acidovorans has been isolated that is specific for the stereospecific hydrolysis of (+)γ-lactam. This so-called (+)γ-lactamase has important applications in biotransformation reactions. The enzyme has been crystallized by vapour-phase diffusion using polyethylene glycol 4000 as a precipitant. Addition of a detergent, β-octylglucoside, was found to be essential for obtaining diffraction-quality crystals. The crystals grow in the space group P1, with unit-cell parameters a = 63.0, b = 93.2, c = 152.4 Å, α = 104.3, β = 92.6, γ = 108.5°, and diffract to 2 Å resolution using synchrotron radiation. Native data from these crystals have been collected to 2.4 Å.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900016838
    Location Call Number Limitation Availability
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    Paper (German National Licenses)
    Fulltext
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