Oxidoreductases;
Acting on the CH-OH group of donors;
With other, known, physiological acceptors
BRITE hierarchy

[sulfatase]-L-serine:S-adenosyl-L-methionine oxidoreductase (3-oxo-L-alanine-forming)

S-adenosyl-L-methionine + a [sulfatase]-L-serine = a [sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine [RN:R12569]

R12569
Reaction

S-adenosyl-L-methionine [CPD:C00019];
[sulfatase]-L-serine [CPD:C22227]

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.

EC 1.1.98.7 created 2020

1  [PMID:10336424]

2  [PMID:14749327]

3  [PMID:18558715]