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Information on EC 2.5.1.30 - heptaprenyl diphosphate synthase and Organism(s) Bacillus subtilis and UniProt Accession P31112

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IUBMB Comments
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.
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Bacillus subtilis
UNIPROT: P31112 not found.
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
heptaprenyl diphosphate synthase, hepps, heptaprenyl pyrophosphate synthetase, heppps, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heptaprenyl pyrophosphate synthetase
-
heptaprenylpyrophosphate synthetase
-
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
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
-
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
-
-
-
?
(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
-
-
-
?
(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
-
-
-
?
(2E,6E)-farnesyl diphosphate + but-3-enyl diphosphate
diphosphate + E-norgeranylgeranyl diphosphate
show the reaction diagram
-
-
-
?
all-trans-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
show the reaction diagram
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
-
-
?
geranyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-hexaprenyl diphosphate
show the reaction diagram
geranyl diphosphate is a poor substrate
-
-
?
geranylgeranyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + all-trans-hexaprenyl diphosphate
show the reaction diagram
-
-
-
?
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
-
wild-type enzyme mainly yields geranylfarnesyl diphosphate (C25, 59%) with a significant amount of heptaprenyl diphosphate (37%)
-
?
additional information
?
-
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 + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
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
recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8
pH 5.5: about 50% of maximal activity, pH 8.0: about 50% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
heptaprenyl diphosphate synthase is involved in the biosynthesis of the side chain of menaquinone-7
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A3F3S0_BACIU
348
0
39460
TrEMBL
-
A3F3N2_BACIU
348
0
39516
TrEMBL
-
A3F3H7_BACIU
251
0
29184
TrEMBL
-
A3F3V8_BACIU
348
0
39518
TrEMBL
-
A3F3H5_BACIU
348
0
39492
TrEMBL
-
A0A8F9SYE4_BACIU
251
0
29095
TrEMBL
-
A3F3N4_BACIU
251
0
29122
TrEMBL
-
A3F3Q3_BACIU
251
0
29154
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
1 * 29000 (enzyme component I) + 1 * 36000 (enzyme component II), SDS-PAGE
29122
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
30000
molecular weight of enzyme component I and enzyme component II is both about 30000 Da, gel filtration
36000
1 * 29000 (enzyme component I) + 1 * 36000 (enzyme component II), SDS-PAGE
39516
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
45000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
molecular weight of enzyme component I and enzyme component II is both about 30000 Da, gel filtration
dimer
heterodimer
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
the hybrid-type combination of component I (Bacillus subtilis) and component II (Bacillus stearothermophilus) gives distinct prenyltransferase activity. The hybrid-type enzyme catalyzes the synthesis of heptaprenyl diphosphate and shows moderate heat stability, which is between those of the natural enzymes from Bacillus subtilis and Bacillus stearothermophilus. There is no possibility of forming a hybrid between the heptaprenyl and hexaprenyl diphosphate synthases
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A79F
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
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
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
mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type
D97A/A79F
mutant enzyme subunit-I(97A)/subunit-II(A79F) forms exclusively geranylgeranyl diphosphate
D97A/A79L
mutant enzyme subunit-I(D97A)/subunit-II(A79L), the final product is farnesylgeranyl diphosphate, increase in the production of geranylgeranyl diphosphate
E128V
mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type
I76G
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
mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type
L94S
9fold lower Vmax values and 7fold higher Km-values for the allylic substrate farnesyl diphosphate compared to wild-type enzyme
N127A
mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type
S80F
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
mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type
V76I
mutant enzyme subunit-I(wild-type)/subunit-II(A79L), octaprenyl diphosphate is the final product with farnesyl diphosphate as allylic primer
V93G
16fold lower Vmax values and 10fold higher Km-values for the allylic substrate farnesyl diphosphate compared to wild-type enzyme
Y103S
Y104S
5fold lower Vmax values and 3fold higher Km-values for the allylic substrate farnesyl diphosphate compared to wild-type enzyme
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the hybrid-type combination of component I (Bacillus subtilis) and component II (Bacillus stearothermophilus) shows moderate heat stability, which is between those of the natural enzymes from Bacillus subtilis and Bacillus stearothermophilus. There is no possibility of forming a hybrid between the heptaprenyl and hexaprenyl diphosphate synthases
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
separation of component I and component II
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
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli, mutant enzymes
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takahashi, I.; Ogura, K.; Seto, S.
Heptaprenyl pyrophosphate synthetase from Bacillus subtilis
J. Biol. Chem.
255
4539-4543
1980
Bacillus subtilis (P31112 and P31114), Bacillus subtilis
Manually annotated by BRENDA team
Sagami, I.; Fujii, H.; Koyama, T.; Ogura, K.
Heptaprenylpyrophosphate synthetase from Bacillus subtilis
Methods Enzymol.
110
199-205
1985
Bacillus subtilis (P31112 and P31114), Bacillus subtilis, Bacillus subtilis PCI-219 (P31112 and P31114)
Manually annotated by BRENDA team
Zhang, Y.W.; Koyama, T.; Ogura, K.
Two cistrons of the gerC operon of Bacillus subtilis encode the two subunits of heptaprenyl diphosphate synthase
J. Bacteriol.
179
1417-1419
1997
Bacillus subtilis (P31112 and P31114), Bacillus subtilis
Manually annotated by BRENDA team
Zhang, Y.W.; Koyama, T.; Marecak, D.M.; Prestwich, G.D.; Maki, Y.; Ogura, K.
Two subunits of heptaprenyl diphosphate synthase of Bacillus subtilis form a catalytically active complex
Biochemistry
37
13411-13420
1998
Bacillus subtilis (P31112 and P31114), Bacillus subtilis
Manually annotated by BRENDA team
Zhang, Y.W.; Li, X.Y.; Sugawara, H.; Koyama, T.
Site-directed mutagenesis of the conserved residues in component I of Bacillus subtilis heptaprenyl diphosphate synthase
Biochemistry
38
14638-14643
1999
Bacillus subtilis (P31112 and P31114), Bacillus subtilis
Manually annotated by BRENDA team
Hirooka, K.; Ohnuma, S.I.; Koike-Takeshita, A.; Koyama, T.; Nishino, T.
Mechanism of product chain length determination for heptaprenyl diphosphate synthase from Bacillus stearothermophilus
Eur. J. Biochem.
267
4520-4528
2000
Bacillus subtilis (P31112 and P31114)
Manually annotated by BRENDA team
Nagaki, M.; Kimura, K.; Kimura, H.; Maki, Y.; Goto, E.; Nishino, T.; Koyama, T.
Artificial substrates of medium-chain elongating enzymes, hexaprenyl- and heptaprenyl diphosphate synthases
Bioorg. Med. Chem. Lett.
11
2157-2159
2001
Bacillus subtilis (P31112 and P31114)
Manually annotated by BRENDA team
Nagaki, M.; Miki, Y.; Nakada, M.; Kawakami, J.; Kitahara, H.; Maki, Y.; Gotoh, Y.; Nishino, T.; Koyama, T.
Substrate specificities of several prenyl chain elongating enzymes with respect to 4-methyl-4-pentenyl diphosphate
Biosci. Biotechnol. Biochem.
68
2070-2075
2004
Bacillus subtilis (P31112 and P31114)
Manually annotated by BRENDA team
Suzuki, T.; Zhang, Y.W.; Koyama, T.; Sasaki, D.Y.; Kurihara, K.
Direct observation of substrate-enzyme complexation by surface forces measurement
J. Am. Chem. Soc.
128
15209-15214
2006
Bacillus subtilis (P31112 and P31114)
Manually annotated by BRENDA team
Ito, M.; Kobayashi, M.; Koyama, T.; Ogura, K.
Stereochemical analysis of prenyltransferase reactions leading to (2)- and (E)-polyprenyl chains
Biochemistry
26
4745-4750
1987
Bacillus subtilis (P31112 and P31114)
Manually annotated by BRENDA team
Zhang, Y.W.; Li, X.Y.; Koyama, T.
Chain length determination of prenyltransferases: both heteromeric subunits of medium-chain (E)-prenyl diphosphate synthase are involved in the product chain length determination
Biochemistry
39
12717-12722
2000
Bacillus subtilis (P31112 and P31114), Bacillus subtilis
Manually annotated by BRENDA team