Literature summary for 2.8.1.1 extracted from

Kaur, Y.; Ybarra, J.; Horowitz, P.M.
Active rhodanese lacking nonessential sulfhydryl groups has increased hydrophobic exposure not observed in wild-type enzyme (2004), Protein J., 23, 255-261.

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Protein Variants

Protein Variants	Comment	Organism
C3S	mutant enzyme is fully active but less stable than wild-type enzyme, mutant enzyme has more easily exposed apparent hydrophobic surfaces than wild-type enzyme	Bos taurus

General Stability

General Stability	Organism
mutant enzyme C3S is inactivated by bis(1,8-anilinonaphthalenesulfonate) in the light, bis(1,8-anilinonaphthalenesulfonate) is photo-incorporated into the C-terminal domain of C3S and makes the mutant enzyme less stable, binding to wild-type enzyme is very slow	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Synonyms

Synonyms	Comment	Organism
rhodanese	-	Bos taurus

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Release 2023.1 (January 2023)