Literature summary for 2.5.1.90 extracted from

Han, X.; Chen, C.C.; Kuo, C.J.; Huang, C.H.; Zheng, Y.; Ko, T.P.; Zhu, Z.; Feng, X.; Wang, K.; Oldfield, E.; Wang, A.H.; Liang, P.H.; Guo, R.T.; Ma, Y.
Crystal structures of ligand-bound octaprenyl pyrophosphate synthase from Escherichia coli reveal the catalytic and chain-length determining mechanisms (2015), Proteins, 83, 37-45.

Cloned(Commentary)

Cloned (Comment)	Organism
amino acid sequence comparison, recombinant cloning into vector pET46 Ek/LIC and expression of His-tagged enzyme in Escherichia coli strain BL21trxB (DE3)	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant His-tagged enzyme in apo-form and in complexes with isopentenyl diphosphate and a farnesyl diphosphate thio-analogue, FsPP, sitting drop vapor diffusion method, mixing of 0.002 ml of 3 mg/ml protein in 25 mM Tris-HCl, pH 7.5, and 150 mM NaCl, with 0.002 ml of reservoir solution containing 0.3 M magnesium chloride, 0.1 M Tris-HCl, pH 8.5, and 24% w/v PEG 3350, and equilibration against 0.3 ml of reservori solution, 22°C, 3-4 days, X-ray diffraction structure determination and analysis at resolutions of 2.2-2.6 A	Escherichia coli

Crystallization (Comment)

Organism

purified recombinant His-tagged enzyme in apo-form and in complexes with isopentenyl diphosphate and a farnesyl diphosphate thio-analogue, FsPP, sitting drop vapor diffusion method, mixing of 0.002 ml of 3 mg/ml protein in 25 mM Tris-HCl, pH 7.5, and 150 mM NaCl, with 0.002 ml of reservoir solution containing 0.3 M magnesium chloride, 0.1 M Tris-HCl, pH 8.5, and 24% w/v PEG 3350, and equilibration against 0.3 ml of reservori solution, 22°C, 3-4 days, X-ray diffraction structure determination and analysis at resolutions of 2.2-2.6 A

Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
EDTA	-	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
(2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate	Escherichia coli	-	5 diphosphate + all-trans-octaprenyl diphosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AD57	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21trxB (DE3) by nickel affinity and anion exchange chromatography, followed by dialysis	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate	-	Escherichia coli	5 diphosphate + all-trans-octaprenyl diphosphate	-	?
additional information	at the bottom of the active-site tunnel, residues M123 and M135 act in concert to form a wall which determines the final chain length, substrate binding and enzyme-ligand structure analysis, overview	Escherichia coli	?	-	?

Subunits

Subunits	Comment	Organism
More	structure comparisons	Escherichia coli

Synonyms

Synonyms	Comment	Organism
C40-OPP	-	Escherichia coli
long-chain trans-prenyltransferase	-	Escherichia coli
octaprenyl pyrophosphate synthase	-	Escherichia coli
Opp	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Escherichia coli

General Information

General Information	Comment	Organism
evolution	octaprenyl diphosphate synthase, OPP, belongs to the trans-prenyltransferase class of protein	Escherichia coli
additional information	enzyme homology modeling, overview. (2E,6E)-Farnesyl diphosphate is bound to the first DDXXD motif, and isopentenyl diphosphate is bound to several cationic residues (e.g. Arg, Lys, and His) via diphosphate, but not to the second DDXXD motif. The enzyme contains an elongated tunnel-shaped crevice as the active site to accommodate its reactants and product	Escherichia coli
physiological function	the enzyme catalyzes consecutive condensation reactions of one allylic substrate farnesyl diphosphate and five homoallylic substrate isopentenyl diphosphate molecules to form a C40 long-chain product octaprenyl diphosphate, which serves as a side chain of ubiquinone and menaquinone	Escherichia coli