Literature summary for 1.1.3.6 extracted from

Caldinelli, L.; Iametti, S.; Barbiroli, A.; Fessas, D.; Bonomi, F.; Piubelli, L.; Molla, G.; Pollegioni, L.
Relevance of the flavin binding to the stability and folding of engineered cholesterol oxidase containing noncovalently bound FAD (2008), Protein Sci., 17, 409-419.

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Protein Variants

Protein Variants	Comment	Organism
H69A	mutation results in a significant decrease in activity, in the midpoint redox potential of the flavin, and in stability with respect to the wild-type enzyme, but does not modify the overall structure of the enzyme	Brevibacterium sterolicum

Organic Solvent Stability

Organic Solvent	Comment	Organism
urea	the apoprotein of the mutant H69A lacks the characteristic tertiary structure of the holoprotein and displays larger hydrophobic surfaces. Its urea-induced unfolding does not occur by a simple two-state mechanism and is largely nonreversible. Minor alterations in the flavin binding region are evident between the native and the refolded proteins, and are likely responsible for the low refolding yield observed	Brevibacterium sterolicum

Organism

Organism	UniProt	Comment	Textmining
Brevibacterium sterolicum	-	-	-

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Brevibacterium sterolicum

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Release 2023.1 (January 2023)