EC Number |
Metals/Ions |
Reference |
---|
4.1.99.14 | 4Fe-4S |
- |
715287 |
4.1.99.14 | Fe |
iron-sulfur enzyme, 2.9 Fe per enzyme |
692777 |
4.1.99.14 | Fe2+ |
contains a [4Fe-4S] cluster |
727295 |
4.1.99.14 | Fe2+ |
iron-sulfur protein, the aerobically purified apo-SplG forms a homodimer, which contains one [4Fe-4S] cluster per monomer unit after reconstitution to the holoform |
680717 |
4.1.99.14 | Fe2+ |
metalloenzyme, the enzyme uses a [4Fe-4S]1+ cluster to reduce the S-adenosyl-L-methionine generating a catalytic 5'-deoxyadenosyl radical |
726998 |
4.1.99.14 | Fe2+ |
the enzyme is an S-adenosylmethionine-dependent [4Fe-4S]2+ protein, spectral analysis, overview |
680685 |
4.1.99.14 | Fe2+ |
the enzyme uses a [4Fe-4S]1+ cluster and S-adenosyl-L-methionine to initiate the repair reaction |
728401 |
4.1.99.14 | Fe2+ |
the enzyme uses a [4Fe-4S]1+ cluster to reduce the S-adenosyl-L-methionine generating a catalytic 5'-deoxyadenosyl radical |
727020 |
4.1.99.14 | Fe2+ |
the purified enzyme contains between 2.3 and 3.1 iron atoms per protein molecule. A [3Fe-4S]+ cluster accounts for 3-4% of the iron, and a [4Fe-4S]+ cluster accounts for 34-45% of total iron. The SP lyase can be photoreduced under anaerobic conditions in the presence of DTT, tris(hydroxymethyl)aminomethane, and 5-deazariboflavin |
715668 |
4.1.99.14 | Fe2+ |
utilizes a tricysteine CXXXCXXC motif to harbor a [4Fe-4S] cluster |
727074 |