Literature summary for 1.8.3.7 extracted from

Appel, M.J.; Meier, K.K.; Lafrance-Vanasse, J.; Lim, H.; Tsai, C.L.; Hedman, B.; Hodgson, K.O.; Tainer, J.A.; Solomon, E.I.; Bertozzi, C.R.
Formylglycine-generating enzyme binds substrate directly at a mononuclear Cu(I) center to initiate O2 activation (2019), Proc. Natl. Acad. Sci. USA, 116, 5370-5375 .

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Application

Application	Comment	Organism
biotechnology	the enzyme is an enabling biotechnology tool due to the robust utility of the aldehyde product as a bioconjugation handle in recombinant proteins	Streptomyces coelicolor

Crystallization (Commentary)

Crystallization (Comment)	Organism
X-ray crystal structure of Cu-bound enzyme at a resolution of 2.2 A	Streptomyces coelicolor

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cu(I)	the enzyme binds the substrate directly at a mononuclear Cu(I) center to initiate O2 activation. The copper atom is coordinated by two active-site cysteine residues in a nearly linear geometry	Streptomyces coelicolor

Organism

Organism	UniProt	Comment	Textmining
Streptomyces coelicolor	Q9F3C7	-	-
Streptomyces coelicolor ATCC BAA-471	Q9F3C7	-	-

Synonyms

Synonyms	Comment	Organism
FGE	-	Streptomyces coelicolor

General Information

General Information	Comment	Organism
physiological function	the enzyme is required for the posttranslational activation of type I sulfatases by oxidation of an active-site cysteine to Ca-formylglycine	Streptomyces coelicolor

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Release 2023.1 (January 2023)