Structural highlights
Function
ANSME_CLOP1 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.[1] [2] [3]
References
- ↑ Berteau O, Guillot A, Benjdia A, Rabot S. A new type of bacterial sulfatase reveals a novel maturation pathway in prokaryotes. J Biol Chem. 2006 Aug 11;281(32):22464-70. Epub 2006 Jun 9. PMID:16766528 doi:M602504200
- ↑ Benjdia A, Leprince J, Guillot A, Vaudry H, Rabot S, Berteau O. Anaerobic sulfatase-maturating enzymes: radical SAM enzymes able to catalyze in vitro sulfatase post-translational modification. J Am Chem Soc. 2007 Mar 28;129(12):3462-3. Epub 2007 Mar 3. PMID:17335281 doi:10.1021/ja067175e
- ↑ Benjdia A, Subramanian S, Leprince J, Vaudry H, Johnson MK, Berteau O. Anaerobic sulfatase-maturating enzymes, first dual substrate radical S-adenosylmethionine enzymes. J Biol Chem. 2008 Jun 27;283(26):17815-26. doi: 10.1074/jbc.M710074200. Epub 2008, Apr 11. PMID:18408004 doi:10.1074/jbc.M710074200
