Literature summary for 1.13.11.20 extracted from

Li, J.; Koto, T.; Davis, I.; Liu, A.
Probing the Cys-Tyr cofactor biogenesis in cysteine dioxygenase by the genetic incorporation of fluorotyrosine (2019), Biochemistry, 58, 2218-2227 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of uncross-linked F2-Tyr157 CDO and mature wild-type CDO in complex with both L-cysteine and nitric oxide. The active site Cys93, rather than the Tyr157, is well-aligned to be oxidized should the normal oxidation reaction uncouple	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	expression of purely uncross-linked human CDO due to site-specific incorporation of 3,5-difluoro-L-tyrosine Cys-Tyr at the cross-linking site through a genetic code expansion strategy	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q16878	-	-

General Information

General Information	Comment	Organism
metabolism	the first target to oxidize during the iron-assisted Cys-Tyr cofactor biogenesis is Cys93	Homo sapiens

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Release 2023.1 (January 2023)