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Literature summary for 1.1.1.1 extracted from

  • Barzegar, A.; Moosavi-Movahedi, A.A.; Rezaei-Zarchi, S.; Saboury, A.A.; Ganjali, M.R.; Norouzi, P.; Hakimelahi, G.H.; Tsai, F.Y.
    The mechanisms underlying the effect of alpha-cyclodextrin on the aggregation and stability of alcohol dehydrogenase (2008), Biotechnol. Appl. Biochem., 49, 203-211.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Equus caballus
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Source Tissue

Source Tissue Comment Organism Textmining
liver
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Equus caballus
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Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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alpha-cyclodextrin causes thermal stabilization and delays the onset of secondary structural unfolding and aggregation by approx. 10°C and the midpoint temperatures by more than 5°C. alpha-Cyclodextrin diminishes the deactivation of the enzyme, decreasing the deactivation constant by more than 50%, and clearly reveals the stabilization of the enzyme not only structurally but also kinetically at higher temperatures Equus caballus