| EC |
1.1.98.7 |
| Accepted name: |
serine-type anaerobic sulfatase-maturating enzyme |
| Reaction: |
S-adenosyl-L-methionine + a [sulfatase]-L-serine = a [sulfatase]-3-oxo-L-alanine + 5′-deoxyadenosine + L-methionine |
| Glossary: |
3-oxo-L-alanine = (S)-formylglycine = (S)-Cα-formylglycine = FGly |
| Other name(s): |
atsB (gene name) |
| Systematic name: |
[sulfatase]-L-serine:S-adenosyl-L-methionine oxidoreductase (3-oxo-L-alanine-forming) |
| 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, cysteine-type anaerobic sulfatase-maturating enzyme. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
| References: |
| 1. |
Szameit, C., Miech, C., Balleininger, M., Schmidt, B., von Figura, K. and Dierks, T. The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase. J. Biol. Chem. 274 (1999) 15375–15381. [PMID: 10336424] |
| 2. |
Fang, Q., Peng, J. and Dierks, T. Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB. J. Biol. Chem. 279 (2004) 14570–14578. [PMID: 14749327] |
| 3. |
Grove, T.L., Lee, K.H., St Clair, J., Krebs, C. and Booker, S.J. In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters. Biochemistry 47 (2008) 7523–7538. [PMID: 18558715] |
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| [EC 1.1.98.7 created 2020] |
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