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Literature summary for 2.4.2.28 extracted from

  • Cacciapuoti, G.; Fuccio, F.; Petraccone, L.; Del Vecchio, P.; Porcelli, M.
    Role of disulfide bonds in conformational stability and folding of 5-deoxy-5-methylthioadenosine phosphorylase II from the hyperthermophilic archaeon Sulfolobus solfataricus (2012), Biochim. Biophys. Acta, 1824, 1136-1143.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant SsMTAPII and its C262S and C259S/C261S mutant forms are expressed in Escherichia coli BL21 (lDE3) cells Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
C259S/C261S in contrast wo wild-type C262S and C259S/C261S mutants show complete thermal denaturation curves with sigmoidal transitions centered at 102°C and 99°C respectively. Under reducing conditions these values decrease by 4°C and 8°C respectively, highlighting the important role exerted by the CXC disulfide on enzyme thermostability. The double mutant (the mutant lacking the structural CXC motif), has more impact on the thermostability of SsMTAPII than the single mutant Saccharolobus solfataricus
C262S in contrast wo wild-type C262S and C259S/C261S mutants show complete thermal denaturation curves with sigmoidal transitions centered at 102°C and 99°C respectively. Under reducing conditions these values decrease by 4°C and 8°C respectively, highlighting the important role exerted by the CXC disulfide on enzyme thermostability Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
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-
-

Purification (Commentary)

Purification (Comment) Organism
using heat-treatment and MTA-Sepharose chromatography Saccharolobus solfataricus

Subunits

Subunits Comment Organism
hexamer
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Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
5'-deoxy-5'-methylthioadenosine phosphorylase II
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Saccharolobus solfataricus