Literature summary for 1.1.3.9 extracted from

Li, J.; Davis, I.; Griffith, W.P.; Liu, A.
Formation of monofluorinated radical cofactor in galactose oxidase through copper-mediated C-F bond scission (2020), J. Am. Chem. Soc., 142, 18753-18757 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of the GAOV Cl2-Tyr272, and F2-Tyr272 incorporated variants at 1.48, 1.23, and 1.80 A resolution, respectively. Only one halogen atom remains in the cofactor. The structurally defined catalytic center with genetic unnatural tyrosine substitution is in the radical containing form as in the wild-type, i.e., Cu(II)-(Cl-Tyr radical-Cys) or Cu(II)-(F-Tyr radical-Cys). Thus an C-F/C-Cl bond cleavage is mediated by a mononuclear copper center	Fusarium graminearum

Crystallization (Comment)

Organism

crystal structures of the GAOV Cl2-Tyr272, and F2-Tyr272 incorporated variants at 1.48, 1.23, and 1.80 A resolution, respectively. Only one halogen atom remains in the cofactor. The structurally defined catalytic center with genetic unnatural tyrosine substitution is in the radical containing form as in the wild-type, i.e., Cu(II)-(Cl-Tyr radical-Cys) or Cu(II)-(F-Tyr radical-Cys). Thus an C-F/C-Cl bond cleavage is mediated by a mononuclear copper center

Fusarium graminearum

Protein Variants

Protein Variants	Comment	Organism
additional information	genetic incorporation of 3,5-dichlorotyrosine (Cl2-Tyr) and 3,5-difluorotyrosine (F2-Tyr) to replace Tyr272 in the GAOV variant (i.e. A3.E7) optimized for expression through directed evolution. The proteins with an unnatural tyrosine residue are catalytically competent	Fusarium graminearum

Organism

Organism	UniProt	Comment	Textmining
Fusarium graminearum	P0CS93	-	-

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Release 2023.1 (January 2023)