Cloned (Comment) | Organism |
---|---|
the two subunits (subunit I and subunit II) of the HepPP synthase are overproduced in Escherichia coli cells respectively and purified. These subunits are modified with six histidines (polyhistidine) at the N-terminal | Bacillus subtilis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | 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 | Bacillus subtilis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | P31112 and P31114 | P31112: subunit 1, P31114: subunit 2 | - |
Purification (Comment) | Organism |
---|---|
the two subunits (subunit I and subunit II) of the HepPP synthase are overproduced in Escherichia coli cells respectively and purified. These subunits are modified with six histidines (polyhistidine) at the N-terminal | Bacillus subtilis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate | initially the substrate farnesyl diphosphate binds to subunit II using Mg2+, followed by the formation of the subunit I-farnesyl diphosphate-Mg2+-subunit II complex | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate | initially the substrate farnesyl diphosphate binds to subunit II using Mg2+, followed by the formation of the subunit I-farnesyl diphosphate-Mg2+-subunit II complex | Bacillus subtilis | 4 diphosphate + all-trans-heptaprenyl diphosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
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 | Bacillus subtilis |
Synonyms | Comment | Organism |
---|---|---|
HepPP synthase | - |
Bacillus subtilis |