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(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate
a common mechanism controls the product chain length of both short-chain and medium-chain prenyl diphosphate synthases. In wild-type heptaprenyl diphosphate synthase, the prenyl chain can grow on the surface of the small residues at positions 79 and 80, and the elongation is precisely blocked at the length of C35 by Ile76
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate
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. Component I is involved in allylic substrate recognition
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate
initially the substrate farnesyl diphosphate binds to subunit II using Mg2+, followed by the formation of the subunit I-farnesyl diphosphate-Mg2+-subunit II complex
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate
the C-C bond formation in the heptaprenyl diphosphate synthase reaction takes place at the si face of the double bond of isopentenyl diphosphate
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(2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate
3 diphosphate + all-trans-hexaprenyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + 3-ethylbut-3-enyl diphosphate
diphosphate + (all-E)-3-ethyl-7,11,15-trimethylhexadeca-2,6,10,14-tetraenyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + 3-propylbut-3-enyl diphosphate
diphosphate + (all-E)-3-propyl-7,11,15-trimethylhexadeca-2,6,10,14-tetraenyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
(2E,6E)-farnesyl diphosphate + but-3-enyl diphosphate
diphosphate + (E)-norgeranylgeranyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + but-3-enyl diphosphate
diphosphate + E-norgeranylgeranyl diphosphate
-
-
-
?
all-trans-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
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
geranyl diphosphate is a poor substrate
-
-
?
geranylgeranyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + all-trans-hexaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 3 isopentenyl diphosphate
3 diphosphate + all-trans-heptaprenyl diphosphate
geranylgeranyl diphosphate + isopentenyl diphosphate
diphosphate + all-trans-heptaprenyl diphosphate + geranylfarnesyl diphosphate
-
wild-type enzyme mainly yields geranylfarnesyl diphosphate (C25, 59%) with a significant amount of heptaprenyl diphosphate (37%)
-
?
additional information
?
-
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
heptaprenyl diphosphate synthase is involved in the biosynthesis of the side chain of menaquinone-7
-
-
?
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
synthesis of all-trans-heptaprenyl diphosphate, which is precursor for the side chain of menaquinone-7
-
-
?
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
initially the substrate farnesyl diphosphate binds to subunit II using Mg2+, followed by the formation of the subunit I-farnesyl diphosphate-Mg2+-subunit II complex
-
-
?
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
the C-C bond formation in the heptaprenyl diphosphate synthase reaction takes place at the si face of the double bond of isopentenyl diphosphate
-
-
?
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
the enzyme reaction proceeds with an elimination of 2-pro-R hydrogen of isopentenyl diposphate without accumulation of any prenyl diphosphate shorter than C35
-
-
?
(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-heptaprenyl diphosphate
wild-type enzyme mainly produces heptaprenyl diphosphate (C35, molar ratio, 73%) and does not yield any product longer than heptaprenyl diphosphate
-
-
?
geranylgeranyl diphosphate + 3 isopentenyl diphosphate
3 diphosphate + all-trans-heptaprenyl diphosphate
-
-
-
?
geranylgeranyl diphosphate + 3 isopentenyl diphosphate
3 diphosphate + all-trans-heptaprenyl diphosphate
-
-
-
-
?
geranylgeranyl diphosphate + 3 isopentenyl diphosphate
3 diphosphate + all-trans-heptaprenyl diphosphate
the enzyme reaction proceeds with an elimination of 2-pro-R hydrogen of isopentenyl diphosphate without accumulation of any prenyl diphosphate shorter than C35. Poor activity of geranylneryl diphosphate contrast with the high activity of the all-trans isomer is consistent with the proposal that this enzyme catalyzes condensations resulting in trans products
-
-
?
additional information
?
-
dimethylallyl diphosphate and geranyl diphosphate, are almost inactive as substrates
-
-
?
additional information
?
-
-
dimethylallyl diphosphate and geranyl diphosphate, are almost inactive as substrates
-
-
?
additional information
?
-
neither dimethylallyl diphosphate nor geranyl diphosphate is active as primer
-
-
?
additional information
?
-
-
neither dimethylallyl diphosphate nor geranyl diphosphate is active as primer
-
-
?
additional information
?
-
no activity with 3-butylbut-3-enyl diphosphate, norfarnesyl diphosphate or norgeranylgeranyl diphosphate
-
-
?
additional information
?
-
norfarnesyl diphosphate is not accepted as substrate
-
-
?
additional information
?
-
the enzyme does not catalyze a reaction between isopentenyl diphosphate and either dimethylallyl or geranyl diphosphate
-
-
?
additional information
?
-
-
the enzyme does not catalyze a reaction between isopentenyl diphosphate and either dimethylallyl or geranyl diphosphate
-
-
?
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0.0053 - 0.0741
(2E,6E)-farnesyl diphosphate
0.0083 - 0.0568
geranylgeranyl diphosphate
0.0128 - 0.0259
isopentenyl diphosphate
0.0053
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme L107S
0.0056
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme E128V
0.0064
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme D73A
0.0069
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme D97A
0.0071
(2E,6E)-farnesyl diphosphate
pH 8.5, 30°C
0.0072
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, wild-type enzyme
0.0072
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme K130I
0.0072
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme L102S
0.0077
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, wild-type enzyme
0.0082
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme N127A
0.0084
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme T76V
0.0085
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-I(wild-type)/subunit-B(A79F)
0.0098
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme Y103S
0.0103
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme S100G
0.0116
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-I(wild-type)/subunit-B(I76G)
0.0124
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-I(wild-type)/subunit-II(A79L)
0.0133
(2E,6E)-farnesyl diphosphate
pH 7.5, 37°C
0.0133
(2E,6E)-farnesyl diphosphate
-
pH 7.5, 37°C
0.02
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme Y104S
0.0508
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme L94S
0.0741
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme V93G
0.0083
geranylgeranyl diphosphate
pH 7.5, 37°C
0.0083
geranylgeranyl diphosphate
-
pH 7.5, 37°C
0.0085
geranylgeranyl diphosphate
pH 8.5, 30°C
0.0168
geranylgeranyl diphosphate
pH 8.5, 37°C, wild-type enzyme
0.0198
geranylgeranyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-I(wild-type)/subunit-II(I76G)
0.0344
geranylgeranyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-I(wild-type)/subunit-II(A79L)
0.0568
geranylgeranyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-I(wild-type)/subunit-II(A79F)
0.0128
isopentenyl diphosphate
pH 7.5, 37°C
0.0128
isopentenyl diphosphate
-
pH 7.5, 37°C
0.0134
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme K130I
0.0142
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme S100G
0.0143
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-I(wild-type)/subunit-II(A79F)
0.0156
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme D97A
0.0161
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme D73A
0.0167
isopentenyl diphosphate
pH 8.5, 30°C
0.0167
isopentenyl diphosphate
pH 8.5, 37°C, wild-type enzyme
0.0167
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme Y104S
0.0172
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme E128V
0.0175
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme L107S
0.0183
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme T76V
0.0188
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme Y103S
0.0194
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme L94S
0.0194
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme N127A
0.0198
isopentenyl diphosphate
pH 8.5, 37°C, wild-type enzyme
0.0203
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme L102S
0.0214
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-I(wild-type)/subunit-II(I76G)
0.0226
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme V93G
0.0259
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-I(wild-type)/subunit-II(A79L)
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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
Y104S
5fold lower Vmax values and 3fold higher Km-values for the allylic substrate farnesyl diphosphate compared to wild-type enzyme
D97A
mutant enzyme subunit-I(D97A)/subunit-II(wild-type), major products: geranylgeranyl diphosphate, farnesylgeranyl diphosphate, hexaprenyl diphosphate, heptaprenyl diphosphate
D97A
reaction products have marked differences in chain length distribution from the wild-type enzyme. D97A produces larger amounts of shorter chain prenyl diphosphates
Y103S
mutant enzyme subunit-I(Y103S)/subunit-II(wild-type), final product is octaprenyl diphosphate
Y103S
reaction products have marked differences in chain length distribution from the wild-type enzyme. Y103S gives octaprenyl diphosphate (C40) as the final product
additional information
elucidation of the mechanism of chain length determination of Bacillus stearothermophilus HepPS by site-directed mutagenesis
additional information
several amino acid residues in the larger subunits Bacillus subtilis heptaprenyl diphosphate synthase are selected for substitutions by site-directed mutagenesis and examined by combination with the corresponding wild type or mutated smaller subunits
additional information
-
several amino acid residues in the larger subunits Bacillus subtilis heptaprenyl diphosphate synthase are selected for substitutions by site-directed mutagenesis and examined by combination with the corresponding wild type or mutated smaller subunits
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
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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
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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)
brenda
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)
brenda
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)
brenda
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)
brenda
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
brenda