EC Number   |
Metals/Ions |
Reference |
|---|
    2.8.1.6 | Mn2+ |
enhances activity |
645589 |
| 2.8.1.6 | S2- |
enhances activity |
645605 |
| 2.8.1.6 | FeCl3 |
enhances activity 3-4fold at 0.1 mM |
645587 |
| 2.8.1.6 | Na2S |
enhances activity 3-4fold at 1 mM |
645587 |
| 2.8.1.6 | Iron |
enzyme contains a (4FE-4S) cluster that is stable during the reaction and bound to S-adenosyl-L-methionine. Additionally, enzyme contains a (2Fe-2S) cluster. About 2/3 of the (2Fe-2S) clusters are degraded by the end of a turnover experiment, degradation is initiated by reduction of the cluster |
661115 |
| 2.8.1.6 | Iron |
enzyme contains two distinct Fe-S cluster binding sites, one site accomodates a (2Fe-2S)2+ cluster with partial noncysteinyl ligation, the other site accomodates a (4Fe-4S)2+ cluster that binds S-adenosyl-L-methionine and undergoes O2-induced degradation |
661114 |
| 2.8.1.6 | Iron |
Fe/S cluster assembly of biotin synthase strongly depends on Isu1 and Isu2 proteins |
673421 |
| 2.8.1.6 | Iron |
Fe/S cluster assembly on Bio2 strongly depends on the Isu1 and Isu2 proteins, Isa proteins are crucial for the in vivo function of biotin synthase but not for the de novo synthesis of its Fe/S clusters. |
673421 |
| 2.8.1.6 | Fe2+ |
highly stimulates |
645610 |
| 2.8.1.6 | Iron |
in a partially purified fraction the presence of a S2- source and Fe2+ converts the predominant [2Fe-2S] into a 1:1 mixture of [2Fe-2S] and [4Fe-4S], reduced [4Fe-4S] is involved in mediating the cleavage of S-adenosylmethionine and reduced [2Fe-2S] is the sulfur source of biotin |
645600 |
