C601F9E188B637604349EBE083CFA63C715944FAD4385AE6EED3DEB47688C11F981FFB136EF106667D39C943240C1276

Involved in 'Cys-type' sulfatase maturation under anaerobic conditions. Catalyzes the post-translational modification of cysteine ('Cys-51' in the arylsulfatase CPF_0221) into 3-oxoalanine (also known as C(alpha)-formylglycine (FGly)), by a free radical chemical mechanism initiated via the reductive cleavage of S-adenosyl-L-methionine (SAM). Is also able to oxidize a serine residue in a synthetic substrate to FGly in vitro, and in a serine variant of a Cys-type sulfatase in vivo, but this activity is not physiological.

Source:http://purl.uniprot.org/SHA-384/C601F9E188B637604349EBE083CFA63C715944FAD4385AE6EED3DEB47688C11F981FFB136EF106667D39C943240C1276

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Predicate	Object
rdf:type	uniprot:Function_Annotation
rdfs:comment	Involved in 'Cys-type' sulfatase maturation under anaerobic conditions. Catalyzes the post-translational modification of cysteine ('Cys-51' in the arylsulfatase CPF_0221) into 3-oxoalanine (also known as C(alpha)-formylglycine (FGly)), by a free radical chemical mechanism initiated via the reductive cleavage of S-adenosyl-L-methionine (SAM). Is also able to oxidize a serine residue in a synthetic substrate to FGly in vitro, and in a serine variant of a Cys-type sulfatase in vivo, but this activity is not physiological.