2.5.1.30: heptaprenyl diphosphate synthase
This is an abbreviated version!
For detailed information about heptaprenyl diphosphate synthase, go to the full flat file.
Word Map on EC 2.5.1.30
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2.5.1.30
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prenyltransferase
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allylic
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synthases
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menaquinone-7
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stearothermophilus
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geranylgeranyl
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hexaprenyl
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medium-chain
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micrococcus
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luteus
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heteromeric
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hepes
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mops
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zwitterionic
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undecaprenyl
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pharmacology
- 2.5.1.30
- prenyltransferase
-
allylic
- synthases
- menaquinone-7
- stearothermophilus
-
geranylgeranyl
-
hexaprenyl
-
medium-chain
-
micrococcus
- luteus
-
heteromeric
- hepes
- mops
-
zwitterionic
- undecaprenyl
- pharmacology
Reaction
+ 4 isopentenyl diphosphate = 4 diphosphate +
Synonyms
HepPP synthase, HepPPS, HepPS, heptaprenyl pyrophosphate synthetase, heptaprenylpyrophosphate synthetase
ECTree
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Subunits
Subunits on EC 2.5.1.30 - heptaprenyl diphosphate synthase
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dimer
heterodimer
additional information
molecular weight of enzyme component I and enzyme component II is both about 30000 Da, gel filtration
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molecular weight of enzyme component I and enzyme component II is both about 30000 Da, gel filtration
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?
x * 24610 (subunit 1) + x * 36172 (subunit 2), calculated from sequence
1 * 29000 (enzyme component I) + 1 * 36000 (enzyme component II), SDS-PAGE
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
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
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
heterodimer
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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
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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
additional information
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
additional information
-
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