Literature summary for 3.1.6.1 extracted from

Dierks, T.; Miech, C.; Hummerjohann, J.; Schmidt, B.; Kertesz, M.A.; von Figura, K.
Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine (1998), J. Biol. Chem., 273, 25560-25564.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in active form in a sulfatase-deficient strain of Pseudomonas aeruginosa, thereby restoring growth on aromatic sulfates as sole sulfur source, and in Escherichia coli.Cysteine is also converted to formylglycine in Escherichia coli	Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
side-chain modification	formylglycine is generated by posttranslational modification of a conserved cysteine residue. Cysteine is also converted to formylglycine when the gene is expressed in Escherichia coli. Substituting the relevant cysteine by a serine codon in the gene of Pseudomonas aeruginosa leads to expression of inactive sulfatase protein, lacking the formylglycine. The machinery catalyzing the modification of the Pseudomonas sulfatase in E. coli therefore accepts cysteine but not serine as a modification substrate	Pseudomonas aeruginosa

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Release 2023.1 (January 2023)