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Information on EC 2.5.1.90 - all-trans-octaprenyl-diphosphate synthase

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IUBMB Comments
This enzyme catalyses the condensation reactions resulting in the formation of all-trans-octaprenyl diphosphate, the isoprenoid side chain of ubiquinone-8 and menaquinone-8. The enzyme adds five isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry
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UNIPROT: Q9X1M1
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
trans-prenyltransferase, octaprenyl diphosphate synthase, octaprenyl pyrophosphate synthase, octaprenyl pyrophosphate, opp synthetase, gbs1789, octaprenyl-diphosphate synthase, long-chain trans-prenyltransferase, long-chain c40 octaprenyl diphosphate synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octaprenyl pyrophosphate synthase
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SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 5 isopentenyl units)
This enzyme catalyses the condensation reactions resulting in the formation of all-trans-octaprenyl diphosphate, the isoprenoid side chain of ubiquinone-8 and menaquinone-8. The enzyme adds five isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-octaprenyl diphosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + all-trans-octaprenyl diphosphate
show the reaction diagram
the polymer all-trans C40-octaprenyl pyrophosphate forms the side chain of ubiquinone that is involved in electron transport system to produce ATP
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0015
(2E,6E)-farnesyl diphosphate
pH 7.5, 25°C
0.002
isopentenyl diphosphate
pH 7.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000023 - 0.0051
(2E,6E)-farnesyl diphosphate
0.005
isopentenyl diphosphate
pH 7.5, 25°C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 85
the enzyme activity at temperatures ranging from 25°C to 85°C exponentially increases with elevated temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
octaprenyl pyrophosphate synthase catalyzes the chain elongation of farnesyl pyrophosphate via consecutive condensation reactions with five molecules of isopentenyl pyrophosphate to generate all-trans C40-octaprenyl pyrophosphate. The polymer forms the side chain of ubiquinone that is involved in electron transport system to produce ATP
physiological function
the enzyme catalyzes consecutive condensation reactions of farnesyl diphosphate with isopentenyl diphosphate to generate octaprenyl diphosphate, which constitutes the side chain of bacterial ubiquinone or menaquinone
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9X1M1_THEMA
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
299
0
33858
TrEMBL
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutants A76Y, A76Y/S77F, F132A/L128A, F132A/L128A/I123A, and F132A/L128A/I123A/D62A to 3.1, 2.7, 3.3, 3.35 and 3.4 A resolution, respectively. Like wildtype OPPs, all mutant structures contain 12 alpha-helices, nine of them surrounding a large central cavity and an elongated tunnel-shaped active site cavity surrounded by four alpha-helices In the crystal structure of the A76Y/S77F mutant, F77 is pushed away by Y76, thereby creating more space between those two large amino acids to accommodate the C20 product. A large F132 residue at the bottom of the tunnel-shaped active site serves as the floor and determines the final product chain length. The substitution of F132 with a small Ala, thereby removing the blockade, leads to the synthesis of a C50 product larger than that produced by the wild-type enzyme
wild-type and mutants F52A, V73A, S77F, F132A, to 2.28, 2.80, 2.85, 2.45 and 2.40 A resolution, respectively. OPPs is composed entirely of alpha-helices joined by connecting loops and is arranged with nine core helices around a large central cavity. An elongated hydrophobic tunnel between D and F alpha-helices contains two DDXXD motifs on the top for substrate binding and is occupied at the bottom with two large residues Phe-52 and Phe-132
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A76Y/S77F
F132A
F132A/L128A
steady-state activity 0.0008 per s. Product chain length C55, C60
F132A/L128A/I123A
steady-state activity 0.00066 per s. Produuct chain length C55 to C75
F132A/L128A/I123A/D62A
products reach C95, beyond the largest chain length generated by all known trans-prenyltransferases. Steady-state activity 0.00061 per s
F52A
product is predominatly C40, like in wild-type
S77F
main product is C20
V73Y
mutation leads to additional accumulation of C30 intermediate
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
Tm-value is above 80°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Guo, R.T.; Kuo, C.J.; Chou, C.C.; Ko, T.P.; Shr, H.L.; Liang, P.H.; Wang, A.H.
Crystal structure of octaprenyl pyrophosphate synthase from hyperthermophilic Thermotoga maritima and mechanism of product chain length determination
J. Biol. Chem.
279
4903-4912
2004
Thermotoga maritima (Q9X1M1), Thermotoga maritima
Manually annotated by BRENDA team
Guo, R.-T.; Kuo, C.-J.; Ko, T.-P.; Chou, C.-C.; Liang, P.-H.; Wang, A.H.J.
A molecular ruler for chain elongation catalyzed by octaprenyl pyrophosphate synthase and its structure-based engineering to produce unprecedented long chain trans-prenyl products
Biochemistry
43
7678-7686
2004
Thermotoga maritima (Q9X1M1), Thermotoga maritima
Manually annotated by BRENDA team
Kuo, T.; Liang, P.
Reaction kinetic pathway of the recombinant octaprenyl pyrophosphate synthase from Thermotoga maritima How is it different from that of the mesophilic enzyme
Biochim. Biophys. Acta
1599
125-133
2002
Thermotoga maritima (Q9X1M1), Thermotoga maritima, Thermotoga maritima DSM 3109 (Q9X1M1)
Manually annotated by BRENDA team