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Literature summary for 3.2.1.93 extracted from

  • Chen, J.H.; Chi, M.C.; Lin, M.G.; Lin, L.L.; Wang, T.F.
    Beneficial effect of sugar osmolytes on the refolding of guanidine hydrochloride-denatured trehalose-6-phosphate hydrolase from Bacillus licheniformis (2015), BioMed Res. Int., 2015, 806847 .
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis
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Bacillus licheniformis Q65MI2
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Bacillus licheniformis 168 Q65MI2
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Renatured (Commentary)

Renatured (Comment) Organism
sorbitol, sucrose, and trehalose at a concentration of 0.75 M improve the refolding yields of guanidine hydrochloride-denatured BlTreA, probably due to the fact that these sugars favor the formation of tertiary architectures. Sorbitol is more effective than any of the other two sugars Bacillus licheniformis
sorbitol, sucrose, and trehalose at a concentration of 0.75 M improve the refolding yields of guanidine hydrochloride-denatured enzyme. Far-UV CD measurements demonstrate the ability of sugar osmolytes to shift the secondary structure of guanidine hydrochloride-denatured enzyme towards near-native conformations. ANS fluorescence intensity measurements reveal a reduction of exposed hydrophobic surfaces upon the treatment of denatured enzyme with sugar osmolytes Bacillus licheniformis

Synonyms

Synonyms Comment Organism
BlTreA
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Bacillus licheniformis
trehalose-6-phosphate hydrolase
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Bacillus licheniformis