ENZYME entry: EC 1.1.98.7
| Accepted Name |
|---|
| Serine-type anaerobic sulfatase-maturating enzyme.
|
| Reaction catalysed |
|---|
| S-adenosyl-L-methionine + a [sulfatase]-L-serine <=> a [sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine |
| Comment(s) |
|---|
- 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.
|
| Cross-references |
|---|
| BRENDA | 1.1.98.7 |
| EC2PDB | 1.1.98.7 |
| ExplorEnz | 1.1.98.7 |
| PRIAM enzyme-specific profiles | 1.1.98.7 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.1.98.7 |
| IUBMB Enzyme Nomenclature | 1.1.98.7 |
| IntEnz | 1.1.98.7 |
| MEDLINE | Find literature relating to 1.1.98.7 |
| MetaCyc | 1.1.98.7 |
| Rhea expert-curated reactions | 1.1.98.7 |
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.1.98.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-