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Information on EC 2.5.1.82 - hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]
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2.5.1.82 hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]IUBMB Comments
The enzyme prefers geranylgeranyl diphosphate to farnesyl diphosphate as an allylic substrate and does not show activity for geranyl diphosphate and prenyl diphosphate. Requires Mg2+ .
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The expected taxonomic range for this enzyme is: Archaea, Eukaryota
Reaction Schemes
Synonyms
(all-E) hexaprenyl diphosphate synthase, (all-trans) hexaprenyl diphosphate synthase, hexaprenyl pyrophosphate synthase, HexPPs, HexPS, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(all-E) hexaprenyl diphosphate synthase
(all-trans) hexaprenyl diphosphate synthase
hexaprenyl pyrophosphate synthase
HexPPs
HexPS
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
geranylgeranyl diphosphate + 2 isopentenyl diphosphate = 2 diphosphate + all-trans-hexaprenyl diphosphate
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
geranylgeranyl-diphosphate:isopentenyl-diphosphate transferase (adding 2 isopentenyl units)
The enzyme prefers geranylgeranyl diphosphate to farnesyl diphosphate as an allylic substrate and does not show activity for geranyl diphosphate and prenyl diphosphate. Requires Mg2+ [1].
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CAS REGISTRY NUMBER
COMMENTARY
83745-07-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
farnesyl diphosphate + 3 isopentenyl diphosphate
3 diphosphate + all-trans-hexaprenyl diphosphate
geranyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-hexaprenyl diphosphate
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-
-
-
?
geranylgeranyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + all-trans-hexaprenyl diphosphate
farnesyl diphosphate + 3 isopentenyl diphosphate
3 diphosphate + all-trans-hexaprenyl diphosphate
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-
-
-
?
farnesyl diphosphate + 3 isopentenyl diphosphate
3 diphosphate + all-trans-hexaprenyl diphosphate
the enzyme prefers geranylgeranyl diphosphate to farnesyl diphosphate as an allylic substrate and does not show activity for geranyl diphosphate and dimethylallyl diphosphate
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-
?
farnesyl diphosphate + 3 isopentenyl diphosphate
3 diphosphate + all-trans-hexaprenyl diphosphate
the enzyme prefers geranylgeranyl diphosphate to farnesyl diphosphate as an allylic substrate and does not show activity for geranyl diphosphate and dimethylallyl diphosphate
-
-
?
geranylgeranyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + all-trans-hexaprenyl diphosphate
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-
-
?
geranylgeranyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + all-trans-hexaprenyl diphosphate
the enzyme prefers geranylgeranyl diphosphate to farnesyl diphosphate as an allylic substrate and does not show activity for geranyl diphosphate and dimethylallyl diphosphate. The main product is hexaprenyl diphosphate (C30) when the concentrations of isopentenyl diphosphate and geranylgeranyl diphosphate are the same. A 10-fold increase in the concentration of isopentenyl diphosphate results in the increased chain length of the products: a significant amount of heptaprenyl diphosphate (C35) is produced, although hexaprenyl diphosphate remains the main product
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-
?
geranylgeranyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + all-trans-hexaprenyl diphosphate
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-
-
?
geranylgeranyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + all-trans-hexaprenyl diphosphate
the enzyme prefers geranylgeranyl diphosphate to farnesyl diphosphate as an allylic substrate and does not show activity for geranyl diphosphate and dimethylallyl diphosphate. The main product is hexaprenyl diphosphate (C30) when the concentrations of isopentenyl diphosphate and geranylgeranyl diphosphate are the same. A 10-fold increase in the concentration of isopentenyl diphosphate results in the increased chain length of the products: a significant amount of heptaprenyl diphosphate (C35) is produced, although hexaprenyl diphosphate remains the main product
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
geranylgeranyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + all-trans-hexaprenyl diphosphate
geranylgeranyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + all-trans-hexaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + all-trans-hexaprenyl diphosphate
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
the enzyme does not show activity without a divalent cation and prefers Mg2+ to other cations such as Mn2+ and Ca2+. At concentrations ranging from 2.5 to 50 mM, the effect of Mg2+ does not change greatly
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Triton X-100
approximately increases the activity of the enzyme 2fold and retains the effect at a similar level through various concentrations from 0.01 to 1%
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HEXPP_SACS2
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
281
0
32275
Swiss-Prot
-
Q975C1_SULTO
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
283
0
32186
TrEMBL
-
A0A0F4Z4K5_TALEM
451
0
48812
TrEMBL
Mitochondrion (Reliability: 3)
A0A564Q3B6_9EURY
350
0
39648
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
D81C and W136E mutant crystals are grown at room temperature by the hanging drop vapor diffusion method from a reservoir solution containing 10% (w/v) polyethyleneglycol 8000, 2.4 M lithium chloride, and 100 mM Tris (pH 8.0). Crystal structure of the homodimeric C30-HexPPs resembles those of other trans-prenyltransferases, including farnesyl pyrophosphate synthase (FPPs) and octaprenyl pyrophosphate synthase
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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introduction of mutations mimicking the chain-length determination region of short-chain enzymes into Sulfolobus solfataricus hexaprenyldiphosphate synthase and characterization of the mutated enzymes. To mimic short-chain enzymes without geranylgeranyl diphosphate synthase type III, the typical amino acid residues observed in the region of enzymes of each group are introduced into Sulfolobus solfataricus hexaprenyldiphosphate synthase. Several successive amino acids before the first aspartate rich motif of Sulfolobus solfataricus hexaprenyldiphosphate synthase are replaced with those of geranylgeranyl diphosphate synthase from Saccharomyces cerevisiae to construct a mutant mimicking geranylgeranyl diphosphate synthase type III. To facilitate purification, (His)6-tag is introduced at the N-terminal of each enzyme. Introduction of the tag does not significantly affect the activity and product specificity of wild-type Sulfolobus solfataricus hexaprenyldiphosphate synthase. The mutant HPS-F1, HPS-GG1, and HPS-GG3, mimicking the chain-length determination regions of eukaryotic farnesyl diphosphate synthases, archaeal geranylgeranyl diphosphate synthases, and eukaryotic geranylgeranyl diphosphate synthases, respectively, sustain high activity comparable to that of the wild type enzyme, except for the facts that HPS-F1 shows reduced activity when (all-trans)-geranylgeranyl diphosphate is used as the allylic substrate (5.5% of the activity of wild-type HPS) and that the activity of HPS-GG3 toward geranyl diphosphate is relatively low (16% of that of wild type hexaprenyldiphosphate synthase). HPS-GG2, possessing the insertion sequence to mimic the chain-length determination region of geranylgeranyl diphosphate synthase type II, significantly decreases enzyme activity toward each allylic substrate (0.8%, 8.3%, and 45% of the activities of wild-type HPS for geranyl diphosphate, farnesyl diphosphate, and (all-trans)-geranylgeranyl diphosphate, respectively). HPS-F2 mimicking the chain-length determination region of farnesyl diphosphate synthase type II, which has both the insertion and the additional mutation before first aspartate rich motif, shows no activity, although the same amounts of enzymes are used. The inactivation of HPS-F2 is considered to arise from either the difference of its insertion sequence from that of HPS-GG2 or the introduction of bulky amino acid before first aspartate rich motif. When geranyldiphosphate and farnesyl diphosphate are used as the allylic substrate, the main product of HPS-F1 is geranylgeranyl diphosphate. A slight amount of C25 product is produced when (all-trans)-geranylgeranyl diphosphate is the substrate. These results and the low reactivity of HPS-F1 with (all-trans)-geranylgeranyl diphosphate indicate that the product specificity of the mutant has been changed into that of geranylgeranyl diphosphate synthase. The conversion of Sulfolobus solfataricus hexaprenyldiphosphate synthase into geranylgeranyl diphosphate synthase, not into farnesyl diphosphate synthase, by the mutation mimicking the chain-length determination region of farnesyl diphosphate synthase type I might reflect the structural difference between hexaprenyldiphosphate synthase and type I farnesyl diphosphate synthases existing at positions other than the mutated sites. HPS-GG1 maily produces hexaprenyldiphosphate, just as wild-type hexaprenyl diphosphate synthase does. It also yields small amounts of C35 product and, when geranyl diphosphate is used as the substrate, the C40 product. Either the conformation of the chain-length determination region or the orientation of the carbon-chain of products in the cavity of the enzyme is considerably different between the archaeal geranylgeranyl diphosphate synthase and hexaprenyl diphosphate synthase
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hemmi, H.; Ikejiri, S.; Yamashita, S.; Nishino, T.
Novel medium-chain prenyl diphosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus
J. Bacteriol.
184
615-620
2002
Saccharolobus solfataricus (Q97W92), Saccharolobus solfataricus P2 (Q97W92)
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Sun, H.Y.; Ko, T.P.; Kuo, C.J.; Guo, R.T.; Chou, C.C.; Liang, P.H.; Wang, A.H.
Homodimeric hexaprenyl pyrophosphate synthase from the thermoacidophilic crenarchaeon Sulfolobus solfataricus displays asymmetric subunit structures
J. Bacteriol.
187
8137-8148
2005
Saccharolobus solfataricus (Q97W92), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97W92)
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Hemmi, H.; Noike, M.; Nakayama, T.; Nishino, T.
Change of product specificity of hexaprenyl diphosphate synthase from Sulfolobus solfataricus by introducing mimetic mutations
Biochem. Biophys. Res. Commun.
297
10961-101
2002
Saccharolobus solfataricus
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