2.5.1.86: trans,polycis-decaprenyl diphosphate synthase
This is an abbreviated version!
For detailed information about trans,polycis-decaprenyl diphosphate synthase, go to the full flat file.
Word Map on EC 2.5.1.86
-
2.5.1.86
-
ubiquinone
-
isoprenoid
-
prenylation
-
isoprene
-
geranyl
-
octaprenyl
-
solanesyl
-
prenyltransferases
-
ubiquinone-10
-
gluconobacter
-
suboxydans
-
corticorubral
-
rubrospinal
-
1-deoxy-d-xylulose
-
drug development
- 2.5.1.86
- ubiquinone
-
isoprenoid
-
prenylation
- isoprene
-
geranyl
-
octaprenyl
-
solanesyl
- prenyltransferases
- ubiquinone-10
-
gluconobacter
- suboxydans
-
corticorubral
-
rubrospinal
- 1-deoxy-d-xylulose
- drug development
Reaction
+ 7 isopentenyl diphosphate = 7 diphosphate +
Synonyms
cis-decaprenyl diphosphate synthase, decaprenyl diphosphate synthase, decaprenyl diphosphate synthase 1, decaprenyl diphosphate synthase 2, DPP synthase, DPPS, DPS1, long-chain prenyl diphosphate synthase, MtDPPS, polyprenyl diphosphate synthase, Rv2361c, SlDPS, Z-decaprenyl-diphosphate synthase
ECTree
Advanced search results
Crystallization
Crystallization on EC 2.5.1.86 - trans,polycis-decaprenyl diphosphate synthase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
crystallization using sparse matrix screens and vapor diffusion, structures of Rv2361c in the apo form, with isopentyl diphosphate bound and with a substrate analogue, citronellyl diphosphate
enzyme in complex with the substrate analogues geranyl S-thiodiphosphate and isopentenyl S-thiodiphosphate, sitting drop vapor diffusion method, using 0.1 M HEPES pH 7.5, 10% (v/v) glycerol, 25% (w/v) PEG 400, 7% (w/v) PEG 3000
in complex with BPH-640, hanging drop vapor diffusion method, using
purified recombinant enzyme in complex with inhibitor BPH-640, X-ray diffraction structure determination and analysis at 1.8-1.9 A resolution
sitting-drop vapour-diffusion method at 25°C. A 1.55 A resolution structure of the enzyme in complex with the substrate analogues geranyl S-thiodiphosphate and isopentenyl S-thiodiphosphate bound to their respective sites in one subunit shows the active-site configuration and the magnesium-coordinated geometry for catalysis