Literature summary for 1.13.11.20 extracted from

Li, J.; Griffith, W.P.; Davis, I.; Shin, I.; Wang, J.; Li, F.; Wang, Y.; Wherritt, D.J.; Liu, A.
Cleavage of a carbon-fluorine bond by an engineered cysteine dioxygenase (2018), Nat. Chem. Biol., 14, 853-860 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of both wild-type and engineered CDO variants containing unnatural tyrosines	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	enzyme contains a posttranslationally generated Cys93-Tyr157 crosslinked cofactor. Incorporating unnatural tyrosines in place of Tyr157 via a genetic method gives catalytically active variants with a thioether bond between Cys93 and the halogen-substituted Tyr157. Crystal structures and data of both wild-type and engineered CDO variants in the purely uncrosslinked form and with a mature cofactor indicate that the enzyme can catalyze oxidative C-F or C-Cl bond cleavage, resulting in a substantial conformational change of both Cys93 and Tyr157 during cofactor assembly	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q16878	-	-

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Release 2023.1 (January 2023)