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Literature summary 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 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.8.3.7 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)

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.3.7 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

EC Number Organism UniProt Comment Textmining
1.8.3.7 Streptomyces coelicolor Q9F3C7
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1.8.3.7 Streptomyces coelicolor ATCC BAA-471 Q9F3C7
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Synonyms

EC Number Synonyms Comment Organism
1.8.3.7 FGE
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 Streptomyces coelicolor

General Information

EC Number General Information Comment Organism
1.8.3.7 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