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Information on EC 2.5.1.29 - geranylgeranyl diphosphate synthase and Organism(s) Rattus norvegicus and UniProt Accession Q6F596

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EC Tree
IUBMB Comments
Some forms of this enzyme will also use geranyl diphosphate and dimethylallyl diphosphate as donors; it will not use larger prenyl diphosphates as efficient donors.
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This record set is specific for:
Rattus norvegicus
UNIPROT: Q6F596
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
geranylgeranyl diphosphate synthase, ggpp synthase, ggdps, ggps1, ggpps1, cotb1, tgfpps, geranylgeranyl diphosphate synthase 1, geranylgeranyl pyrophosphate synthetase, ggppase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
geranylgeranyl diphosphate synthase
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farnesyltransferase
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-
-
-
geranylgeranyl diphosphate synthase
geranylgeranyl pyrophosphate synthase
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-
-
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geranylgeranyl pyrophosphate synthetase
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-
-
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geranylgeranyl-PP synthetase
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-
-
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synthetase, geranylgeranyl pyrophosphate
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alkenyl group transfer
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase
Some forms of this enzyme will also use geranyl diphosphate and dimethylallyl diphosphate as donors; it will not use larger prenyl diphosphates as efficient donors.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-58-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(E,E)-farnesyl diphosphate + isopentenyl diphosphate
diphosphate + geranylgeranyl diphosphate
show the reaction diagram
(E,E)-farnesyl diphosphate + isopentenyl diphosphate
geranylgeranyl diphosphate + diphosphate
show the reaction diagram
dimethylallyl diphosphate + 3 isopentenyl diphosphate
geranylgeranyl diphosphate + 3 diphosphate
show the reaction diagram
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9% of the activity with farnesyl diphosphate
-
-
?
geranyl diphosphate + 2 isopentenyl diphosphate
geranylgeranyl diphosphate + 2 diphosphate
show the reaction diagram
-
15% of the activity with farnesyl diphosphate
-
?
trans,trans-farnesyl diphosphate + isopentenyl diphosphate
diphosphate + geranylgeranyl 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
(E,E)-farnesyl diphosphate + isopentenyl diphosphate
diphosphate + geranylgeranyl diphosphate
show the reaction diagram
the expression level of the active GGPS is at least regulated through the splicing of intron 4b of its gene
-
-
?
(E,E)-farnesyl diphosphate + isopentenyl diphosphate
geranylgeranyl diphosphate + diphosphate
show the reaction diagram
-
-
-
-
?
dimethylallyl diphosphate + 3 isopentenyl diphosphate
geranylgeranyl diphosphate + 3 diphosphate
show the reaction diagram
-
9% of the activity with farnesyl diphosphate
-
-
?
geranyl diphosphate + 2 isopentenyl diphosphate
geranylgeranyl diphosphate + 2 diphosphate
show the reaction diagram
-
15% of the activity with farnesyl diphosphate
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E,E,E)-geranylgeranyl diphosphate
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-
(Z,E,E)-Geranylgeranyl diphosphate
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-
3-azageranylgeranyl diphosphate
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0.0009 mM, 90% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0029 - 0.056
isopentenyl diphosphate
0.00071 - 0.055
trans,trans-farnesyl diphosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000176
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carboxy-terminal deletion mutant DELTA-8
0.0306
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carboxy-terminal deletion mutant DELTA-8
0.0983
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carboxy-terminal deletion mutant DELTA-4
0.117
-
wild-type enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression level of 1a-type mRNA, encoding the active enzyme form is higher than that of 1b-type mRNA, encoding an inactive enzyme form
Manually annotated by BRENDA team
expression level of 1a-type mRNA, encoding the active enzyme form is higher than that of 1b-type mRNA, encoding an inactive enzyme form
Manually annotated by BRENDA team
expression level of 1a-type mRNA, encoding the active enzyme form is higher than that of 1b-type mRNA, encoding an inactive enzyme form
Manually annotated by BRENDA team
expression level of 1a-type mRNA, encoding the active enzyme form is the same as that of 1b-type mRNA, encoding an inactive enzyme form. During testis development the total GGPS mRNSA expression level increases, accompanied by an increase in 1 n-type mRNA, the expression level pf 1a-type mRNA remains kept unchanges
Manually annotated by BRENDA team
expression level of 1a-type mRNA, encoding the active enzyme form is the same as that of 1b-type mRNA, encoding an inactive enzyme form
Manually annotated by BRENDA team
expression level of 1a-type mRNA, encoding the active enzyme form is higher than that of 1b-type mRNA, encoding an inactive enzyme form
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GGPPS_RAT
300
0
34778
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the farnesyl-transferring activities of wild-type GGPS, DELTA-4, DELTA-8 and DELTA-12 carboxyterminal deletion mutants are relatively in a ratio of 1.0, 0.84, 0.26 and 0.0015. Each Km value of the four recombinants are estimated to be 0.00071, 0.002, 0.0028 and 0.055 mM for farnesyl diphosphate and to be 0.0029, 0.0051, 0.056 and above 0.1 mM for isopentenyl diphosphate, respectively. Allylic substrate specificities of these recombinants are estimated by quantitative analysis of the products, revealing that DELTA-8 and DELTA-12 mutants lack the ability to accept dimethylallyl and geranyl diphosphates compared to wild-type GGPS and DELTA-4 mutant
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
KMFTEENE residing on the carboxyl-terminal sequence of GGPS stabilizes the active region involved in the substrate binding and catalysis
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the histidine-tagged deletion mutants (from the carboxyl terminus) (DELTA-4, DELTA-8, DELTA-12 and DELTa-16) are overexpressed in Escherichia coli BL21 (DE3) and purified in a stable form by nickel affinity chromatography except for one mutant DELTA-16
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
protein expressed from 1a-type mRNA is active, protein expressed from 1b-type mRNA is inactive, expression level in HeLa cells, Cos-7 and 293 cells is about 10% relative to that in Escherichia coli. When fusion of beta-galactosidase with C-terminal regions differing between the 1a-type and the 1b-type proteins are expressed in HeLa cells, the expressed fusion proteins are both active but the latter fusion protein expresion level is considerably low compared with the former one
the histidine-tagged deletion mutants (from the carboxyl terminus) (DELTA-4, DELTA-8, DELTA-12 and DELTa-16) are overexpressed in Escherichia coli BL21 (DE3) and purified in a stable form by nickel affinity chromatography except for one mutant DELTA-16
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sagami, H.; Korenaga, T.; Ogura, K.; Steiger, A.; Pyun, H.J.; Coates, R.M.
Studies on geranylgeranyl diphosphate synthase from rat liver: specific inhibition by 3-azageranylgeranyl diphosphate
Arch. Biochem. Biophys.
297
314-320
1992
Rattus norvegicus
Manually annotated by BRENDA team
Matsumura, Y.; Kuzuguchi, T.; Sagami, H.
Relationship between intron 4b splicing of the rat geranylgeranyl diphosphate synthase gene and the active enzyme expression level
J. Biochem.
136
301-312
2004
Rattus norvegicus (Q6F596)
Manually annotated by BRENDA team
Matsumura, Y.; Kidokoro, T.; Miyagi, Y.; Marilingaiah, N.R.; Sagami, H.
The carboxyl-terminal region of the geranylgeranyl diphosphate synthase is indispensable for the stabilization of the region involved in substrate binding and catalysis
J. Biochem.
142
533-537
2007
Rattus norvegicus
Manually annotated by BRENDA team