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Literature summary for 1.1.1.363 extracted from

  • Plomer, J.J.; Gafni, A.
    Renaturation of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides after denaturation in 4 M guanidine hydrochloride: kinetics of aggregation and reactivation (1993), Biochim. Biophys. Acta, 1163, 89-96.
    View publication on PubMed

Organic Solvent Stability

Organic Solvent Comment Organism
guanidine-HCl in 4 M guanidine hydrochloride, the dimeric enzyme dissociates to subunits and is extensively unfolded Leuconostoc mesenteroides

Organism

Organism UniProt Comment Textmining
Leuconostoc mesenteroides
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-
-

Renatured (Commentary)

Renatured (Comment) Organism
in 4 M guanidine-HCl, the dimeric enzyme glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides dissociates to subunits and is extensively unfolded. Rapid dilution of this high guanidine hydrochloride concentration allowes the enzyme to partially renature. The fraction of the enzyme which does not renature aggregates and precipitates out of solution, a process which can not be substantially prevented by stabilizing additives. A renaturation mechanism is described, which involves a bi-unimolecular (subunit association-folding) reaction sequence. This mechanism involves an inactive, dimeric, glucose-6-phosphate dehydrogenase-folding intermediate Leuconostoc mesenteroides

Synonyms

Synonyms Comment Organism
G6PD
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Leuconostoc mesenteroides