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A rationally designed monomeric variant of anthranilate phosphoribosyltransferase from Sulfolobus solfataricus is as active as the dimeric wild-type enzyme but less thermostable.

Schwab, Thomas, Skegro, Darko, Mayans, Olga and Sterner, Reinhard (2008) A rationally designed monomeric variant of anthranilate phosphoribosyltransferase from Sulfolobus solfataricus is as active as the dimeric wild-type enzyme but less thermostable. Journal of molecular biology 376 (2), pp. 506-16.

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Abstract

The anthranilate phosphoribosyltransferase from Sulfolobus solfataricus (ssAnPRT) forms a homodimer with a hydrophobic subunit interface. To elucidate the role of oligomerisation for catalytic activity and thermal stability of the enzyme, we loosened the dimer by replacing two apolar interface residues with negatively charged residues (mutations I36E and M47D). The purified double mutant ...

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Item type:Article
Date:2008
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
18164726PubMed ID
10.1016/j.jmb.2007.11.078DOI
Classification:
NotationType
Anthranilate Phosphoribosyltransferase/metabolismMESH
Calorimetry, Differential ScanningMESH
CatalysisMESH
Crystallography, X-RayMESH
DimerizationMESH
Enzyme StabilityMESH
Escherichia coli/geneticsMESH
Genetic VariationMESH
Hot TemperatureMESH
Hydrogen BondingMESH
HydrophobicityMESH
KineticsMESH
Models, MolecularMESH
MutationMESH
PlasmidsMESH
Protein Structure, SecondaryMESH
Substrate SpecificityMESH
Sulfolobus solfataricus/enzymologyMESH
Dewey Decimal Classification:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:13671
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