Information on EC 2.5.1.30 - heptaprenyl diphosphate synthase

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The expected taxonomic range for this enzyme is: Bacillaceae

EC NUMBER
COMMENTARY hide
2.5.1.30
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RECOMMENDED NAME
GeneOntology No.
heptaprenyl diphosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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heptaprenyl diphosphate biosynthesis
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isoprenoid biosynthesis
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Terpenoid backbone biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 4 isopentenyl units)
This enzyme catalyses the condensation reactions resulting in the formation of all-trans-heptaprenyl diphosphate, the isoprenoid side chain of ubiquinone-7 and menaquinone-7. The enzyme adds four isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry.
CAS REGISTRY NUMBER
COMMENTARY hide
74506-59-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
P31112: subunit 1, P31114: subunit 2; PCI-219
P31112 and P31114
SwissProt
Manually annotated by BRENDA team
P55784: subunit 1, P55785: subunit 2
P55784 and P55785
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
P31112 and P31114
heptaprenyl diphosphate synthase is involved in the biosynthesis of the side chain of menaquinone-7
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 + 3 isopentenyl diphosphate
3 diphosphate + all-trans-hexaprenyl diphosphate
show the reaction diagram
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-
-
-
?
(2E,6E)-farnesyl diphosphate + 3-ethylbut-3-enyl diphosphate
diphosphate + (all-E)-3-ethyl-7,11,15-trimethylhexadeca-2,6,10,14-tetraenyl diphosphate
show the reaction diagram
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-
-
-
?
(2E,6E)-farnesyl diphosphate + 3-propylbut-3-enyl diphosphate
diphosphate + (all-E)-3-propyl-7,11,15-trimethylhexadeca-2,6,10,14-tetraenyl diphosphate
show the reaction diagram
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate + but-3-enyl diphosphate
diphosphate + (E)-norgeranylgeranyl diphosphate
show the reaction diagram
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-
-
-
?
(2E,6E)-farnesyl diphosphate + but-3-enyl diphosphate
diphosphate + E-norgeranylgeranyl diphosphate
show the reaction diagram
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-
-
-
?
all-trans-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
show the reaction diagram
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enzyme component I, enzyme component II, and farnesyl diphosphate-Mg2+ form a ternary complex during catalysis and that neither isopentenyl diphosphate nor the product, heptaprenyl diphosphate, is included in this complex, which probably represents a catalytically active state of the HepPP synthase. Enzyme component I is involved in allylic substrate recognition
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-
?
geranyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-hexaprenyl diphosphate
show the reaction diagram
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geranyl diphosphate is a poor substrate
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-
?
geranylgeranyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + all-trans-hexaprenyl diphosphate
show the reaction diagram
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-
-
-
?
geranylgeranyl diphosphate + 3 isopentenyl diphosphate
3 diphosphate + all-trans-heptaprenyl diphosphate
show the reaction diagram
geranylgeranyl diphosphate + isopentenyl diphosphate
diphosphate + all-trans-heptaprenyl diphosphate + geranylfarnesyl diphosphate
show the reaction diagram
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wild-type enzyme mainly yields geranylfarnesyl diphosphate (C25, 59%) with a significant amount of heptaprenyl diphosphate (37%)
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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enzymatic activity is inhibited by each antiserum against component I or component II, indicating that either component I or component II is confirmed immunochemically to be essential for enzymatic activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0053 - 0.0741
(2E,6E)-farnesyl diphosphate
0.0083 - 0.0568
geranylgeranyl diphosphate
0.0128 - 0.0259
isopentenyl diphosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
7.5 - 9
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recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8
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pH 5.5: about 50% of maximal activity, pH 8.0: about 50% of maximal activity
PDB
SCOP
CATH
ORGANISM
UNIPROT
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)
Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
P31112 and P31114
molecular weight of enzyme component I and enzyme component II is both about 30000 Da, gel filtration
45000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
P31112 and P31114
1 * 29122 (GerC1) + 1 * 39516 (GerC3), GerC3 supplies the sites for the substrate binding and catalytic activity of HepPP synthase, GerC1 plays an auxiliary but essential role in enzymatic catalysis, calculated from sequence
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
separation of component I and component II
P31112 and P31114
the two subunits (subunit I and subunit II) of the HepPP synthase are overproduced in Escherichia coli cells respectively and purified. These subunits are modified with six histidines (polyhistidine) at the N-terminal
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to explore the dynamic interaction of the two dissociable components during catalysis, expression vector systems for the two structural genes, gerC1 and gerC3, are constructed separately, and the two components are overproduced in Escherichia coli cells. Each component is purified homogeneously
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression in Escherichia coli, mutant enzymes
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the two subunits (subunit I and subunit II) of the HepPP synthase are overproduced in Escherichia coli cells respectively and purified. These subunits are modified with six histidines (polyhistidine) at the N-terminal
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to explore the dynamic interaction of the two dissociable components during catalysis, expression vector systems for the two structural genes, gerC1 and gerC3, are constructed separately, and the two components are overproduced in Escherichia coli cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A79F
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mutant enzyme subunit-I(wild-type)/subunit-B(A79F). Comparable kinetic constants with those of the wild-type enzyme. Significantly different pattern of product distribution from that of the wild type. The major product is hexaprenyl diphosphate
A79L
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mutant enzyme subunit-I(wild-type)/subunit-B(A79L). Comparable kinetic constants with those of the wild-type enzyme. Significantly different pattern of product distribution from that of the wild type. The major product is hexaprenyl diphosphate
A79Y
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single replacement to the aromatic residue at the fourth or the fifth position before the first aspartate-rich motif (FARM), mainly yields a C20 product
D73A
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mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type
D97A/A79F
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mutant enzyme subunit-I(97A)/subunit-II(A79F) forms exclusively geranylgeranyl diphosphate
D97A/A79L
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mutant enzyme subunit-I(D97A)/subunit-II(A79L), the final product is farnesylgeranyl diphosphate, increase in the production of geranylgeranyl diphosphate
E128V
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mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type
I76G
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can catalyze condensations of isopentenyl diphosphate beyond the native chain length of C35. With farnesyl diphosphate as allylic substrate the mutant enzyme largely produces (all-trans)-octaprenyl diphosphate (C40, 21%) with a small amount of solanesyl diphosphate (C45, 5.3%). With geranylgeranyl diphosphate as allylic substrate the mutant enzyme yields solanesyl diphosphate (33%) as the main product with a large amount of (all-trans)-octaprenyl diphosphate (21%)
K130I
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mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type
L94S
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9fold lower Vmax values and 7fold higher Km-values for the allylic substrate farnesyl diphosphate compared to wild-type enzyme
N127A
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mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type
S80F
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single replacement to the aromatic residue at the fourth or the fifth position before the first aspartate-rich motif (FARM), mainly yields a C20 product
T76V
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mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type
V76I
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mutant enzyme subunit-I(wild-type)/subunit-II(A79L), octaprenyl diphosphate is the final product with farnesyl diphosphate as allylic primer
V93G
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16fold lower Vmax values and 10fold higher Km-values for the allylic substrate farnesyl diphosphate compared to wild-type enzyme
Y104S
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5fold lower Vmax values and 3fold higher Km-values for the allylic substrate farnesyl diphosphate compared to wild-type enzyme
additional information
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