EC 1.1.98.7 - Serine-type anaerobic sulfatase-maturating enzyme

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IntEnz Enzyme Nomenclature
EC 1.1.98.7

Names

Accepted name:
serine-type anaerobic sulfatase-maturating enzyme
Systematic name:
[sulfatase]-L-serine:S-adenosyl-L-methionine oxidoreductase (3-oxo-L-alanine-forming)

Reaction

Comments:

A bacterial radical S-adenosyl-L-methionine (AdoMet) enzyme that contains three [4Fe-4S] clusters. The enzyme, found in some bacteria, activates a type I sulfatase enzyme (EC 3.1.6.1) by converting a conserved L-serine residue in the active site to a unique 3-oxo-L-alanine residue that is essential for the sulfatase activity. While the enzyme from Klebsiella pneumoniae is specific for L-serine, the enzyme from Clostridium perfringens can also act on L-cysteine, see EC 1.8.98.7.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB

References

  1. Szameit, C., Miech, C., Balleininger, M., Schmidt, B., von Figura, K., Dierks, T.
    The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase.
    J. Biol. Chem. 274 : 15375-15381 (1999). [PMID: 10336424]
  2. Fang, Q., Peng, J., Dierks, T.
    Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB.
    J. Biol. Chem. 279 : 14570-14578 (2004). [PMID: 14749327]
  3. Grove, T. L., Lee, K. H., St Clair, J., Krebs, C., Booker, S. J.
    In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters.
    Biochemistry 47 : 7523-7538 (2008). [PMID: 18558715]

[EC 1.1.98.7 created 2020]