Literature summary for 5.3.3.1 extracted from

Kim, D.H.; Jang, D.S.; Nam, G.H.; Yun, S.; Cho, J.H.; Choi, G.; Lee, H.C.; Choi, K.Y.
Equilibrium and kinetic analysis of folding of ketosteroid isomerase from Comamonas testosteroni (2000), Biochemistry, 39, 13084-13092.

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Organic Solvent Stability

Organic Solvent	Comment	Organism
urea	the recovery of the activity by refolding is not diminished even after a prolonged time, 24 h of exposure to 7 M urea. Reversibility of the folding is assessed by a 100fold dilution of the denatured protein and subsequent determination of enzyme activity. The refolding kinetics as monitored by fluorescence intensity can be described as a fast first-order process followed by a second-order and a subsequent slow first-order processes, there may be a monomeric folding intermediate	Comamonas testosteroni

Organism

Organism	UniProt	Comment	Textmining
Comamonas testosteroni	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
the recovery of the activity by refolding is not diminished even after a prolonged time, 24 h of exposure to 7 M urea	Comamonas testosteroni

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Release 2023.1 (January 2023)