EC Number   |
Subunits |
Reference |
|---|
    2.5.1.30 | ? |
molecular weight of enzyme component I and enzyme component II is both about 30000 Da, gel filtration |
-, 637624 |
| 2.5.1.30 | ? |
x * 24610 (subunit 1) + x * 36172 (subunit 2), calculated from sequence |
704381 |
| 2.5.1.30 | dimer |
1 * 29000 (enzyme component I) + 1 * 36000 (enzyme component II), SDS-PAGE |
637627 |
| 2.5.1.30 | dimer |
this enzyme is composed of two dissociable subunits that exhibit a catalytic activity only when they are associated together in the presence of a cofactor, Mg2+, and a substrate, farnesyl diphosphate. The quartz-crystal microbalance measurement reveals that farnesyl diphosphate is preferentially bound to subunit II in the presence of Mg2+, while the atomic force microscopy measurement shows that the adhesive force between the subunits is observed only in the presence of both Mg2+ and farnesyl diphosphate |
674185 |
| 2.5.1.30 | heterodimer |
1 * 22000 + 1 * 36000, SDS-PAGE, the enzyme consists of a catalytic subunit (HepPPS-2) having two DDXXD motifs and a regulatory subunit (HepPPS-1) that lacks these motifs |
-, 759075 |
| 2.5.1.30 | heterodimer |
1 * 29122 (GerC1) + 1 * 39516 (GerC3), GerC3 supplies the sites for the substrate binding and catalytic activity of HepPP synthase, GerC1 plays an auxiliary but essential role in enzymatic catalysis, calculated from sequence |
637626 |
| 2.5.1.30 | More |
the hybrid-type combination of component I (Bacillus subtilis) and component II (Bacillus stearothermophilus) gives distinct prenyltransferase activity. The hybrid-type enzyme catalyzes the synthesis of heptaprenyl diphosphate and shows moderate heat stability, which is between those of the natural enzymes from Bacillus subtilis and Bacillus stearothermophilus. There is no possibility of forming a hybrid between the heptaprenyl and hexaprenyl diphosphate synthases |
637628, 637631 |
