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(2E,6E)-farnesyl diphosphate + 1 but-3-enyl diphosphate
diphosphate + (E)-norgeranylgeranyl diphosphate
(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 + (all-E)-3,7-diethyl-11,15,19-trimethyleicosa-2,6,10,14,18-pentaenyl 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 + (all-E)-3,7-diethyl-11,15,19-trimethylicosa-2,6,10,14,18-pentaenyl diphosphate
(2E,6E)-farnesyl diphosphate + 3-propylbut-3-enyl diphosphate
?
(2E,6E)-farnesyl diphosphate + but-3-enyl diphosphate
diphosphate + (E)-norgeranylgeranyl diphosphate
(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate
diphosphate + all-trans-hexaprenyl diphosphate + heptaprenyl diphosphate
-
-
-
-
?
geranyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-hexaprenyl diphosphate
geranylgeranyl diphosphate + 2 isopentenyl diphosphate
2 diphosphate + all-trans-hexaprenyl diphosphate
additional information
?
-
(2E,6E)-farnesyl diphosphate + 1 but-3-enyl diphosphate
diphosphate + (E)-norgeranylgeranyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + 1 but-3-enyl diphosphate
diphosphate + (E)-norgeranylgeranyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate
3 diphosphate + all-trans-hexaprenyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate
3 diphosphate + all-trans-hexaprenyl diphosphate
the enzyme prefers farnesyl diphosphate to geranylgeranyl diphosphate (activity is 3fold higher) as an allylic substrate and does not show activity for geranyl diphosphate and dimethylallyl diphosphate
-
-
?
(2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate
3 diphosphate + all-trans-hexaprenyl diphosphate
the enzyme prefers farnesyl diphosphate to geranylgeranyl diphosphate (activity is 3fold higher) as an allylic substrate and does not show activity for geranyl diphosphate and dimethylallyl diphosphate
-
-
?
(2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate
3 diphosphate + all-trans-hexaprenyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + 3 isopentenyl diphosphate
3 diphosphate + all-trans-hexaprenyl diphosphate
-
-
-
-
?
(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 + (all-E)-3,7-diethyl-11,15,19-trimethyleicosa-2,6,10,14,18-pentaenyl 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 + (all-E)-3,7-diethyl-11,15,19-trimethyleicosa-2,6,10,14,18-pentaenyl 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 + (all-E)-3,7-diethyl-11,15,19-trimethylicosa-2,6,10,14,18-pentaenyl 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 + (all-E)-3,7-diethyl-11,15,19-trimethylicosa-2,6,10,14,18-pentaenyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + 3-propylbut-3-enyl diphosphate
?
-
-
-
?
(2E,6E)-farnesyl diphosphate + 3-propylbut-3-enyl 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
-
-
-
?
geranyl diphosphate + 4 isopentenyl diphosphate
4 diphosphate + all-trans-hexaprenyl diphosphate
geranyl diphosphate is a poor substrate
-
-
?
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 + 2 isopentenyl diphosphate
2 diphosphate + all-trans-hexaprenyl diphosphate
the enzyme prefers farnesyl diphosphate to geranylgeranyl diphosphate (activity is 3fold higher) 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
the enzyme prefers farnesyl diphosphate to geranylgeranyl diphosphate (activity is 3fold higher) 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
-
-
-
?
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
?
-
norfarnesyl diphosphate is not accepted as substrate
-
-
?
additional information
?
-
no activity with 3-butylbut-3-enyl diphosphate, norfarnesyl diphosphate or norgeranylgeranyl diphosphate
-
-
?
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1,2-Cyclohexanedione
results in a rapid loss of the component B activity. Component A is resistant, retaining the initial activity almost completely. Farnesyl diphosphate, isopentenyl diphosphate, farnesyl monophosphate and inorganic diphosphate protect the synthase against the inactivation by N-ethylmaleimide, farnesyl diphosphate being the most effective. The presence of Mg2+ is essential for the protection by isopentenyl diphosphate and inorganic diphosphate. For protection of the synthase activity against the inactivation by 2,3-butanedione, the presence of farnesyl diphosphate, isopentenyl diphosphate and Mg2+ is more effective than that of the individual substrates and Mg2+. Inorganic diphosphate provides substantial protection. In the absence of component A, the component B activity is not protected by any substrates or its analogue
2,3-Butanedione
results in a rapid loss of the component B activity. Component A is resistant, retaining the initial activity almost completely. Farnesyl diphosphate, isopentenyl diphosphate, farnesyl monophosphate and inorganic diphosphate protect the synthase against the inactivation by N-ethylmaleimide, farnesyl diphosphate being the most effective. The presence of Mg2+ is essential for the protection by isopentenyl diphosphate and inorganic diphosphate. For protection of the synthase activity against the inactivation by 2,3-butanedione, the presence of farnesyl diphosphate, isopentenyl diphosphate and Mg2+ is more effective than that of the individual substrates and Mg2+. Inorganic diphosphate provides substantial protection. In the absence of component A, the component B activity is not protected by any substrates or its analogue
7,11-dimethyl-2,6,10-dodecatrien-1-yl diphosphate
analogue of farnesyl diphosphate. Two aspartate-rich motifs and the other characteristic motifs in subunit HexB are located around the diphosphate part of 7,11-dimethyl-2,6,10-dodecatrien-1-yl diphosphate
iodoacetamide
results in a rapid loss of the component B activity. Component A is resistant, retaining the initial activity almost completely. Farnesyl diphosphate, isopentenyl diphosphate, farnesyl monophosphate and inorganic diphosphate protect the synthase against the inactivation by N-ethylmaleimide, farnesyl diphosphate being the most effective. The presence of Mg2+ is essential for the protection by isopentenyl diphosphate and inorganic diphosphate. For protection of the synthase activity against the inactivation by 2,3-butanedione, the presence of farnesyl diphosphate, isopentenyl diphosphate and Mg2+ is more effective than that of the individual substrates and Mg2+. Inorganic diphosphate provides substantial protection. In the absence of component A, the component B activity is not protected by any substrates or its analogue
N-ethylmaleimide
results in a rapid loss of the component B activity. Component A is resistant, retaining the initial activity almost completely. Farnesyl diphosphate, isopentenyl diphosphate, farnesyl monophosphate and inorganic diphosphate protect the synthase against the inactivation by N-ethylmaleimide, farnesyl diphosphate being the most effective. The presence of Mg2+ is essential for the protection by isopentenyl diphosphate and inorganic diphosphate. For protection of the synthase activity against the inactivation by 2,3-butanedione, the presence of farnesyl diphosphate, isopentenyl diphosphate and Mg2+ is more effective than that of the individual substrates and Mg2+. Inorganic diphosphate provides substantial protection. In the absence of component A, the component B activity is not protected by any substrates or its analogue
p-chloromercuribenzoate
results in a rapid loss of the component B activity. Component A is resistant, retaining the initial activity almost completely. Farnesyl diphosphate, isopentenyl diphosphate, farnesyl monophosphate and inorganic diphosphate protect the synthase against the inactivation by N-ethylmaleimide, farnesyl diphosphate being the most effective. The presence of Mg2+ is essential for the protection by isopentenyl diphosphate and inorganic diphosphate. For protection of the synthase activity against the inactivation by 2,3-butanedione, the presence of farnesyl diphosphate, isopentenyl diphosphate and Mg2+ is more effective than that of the individual substrates and Mg2+. Inorganic diphosphate provides substantial protection. In the absence of component A, the component B activity is not protected by any substrates or its analogue
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0.0067 - 0.0105
(2E,6E)-farnesyl diphosphate
0.0124 - 0.385
geranylgeranyl diphosphate
0.0137 - 0.0216
isopentenyl diphosphate
0.0067
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-A(wild-type)/subunit-B(A79F)
0.0075
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-A(wild-type)/subunit-B(A79L)
0.0089
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, wild-type enzyme
0.0105
(2E,6E)-farnesyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-A(wild-type)/subunit-B(V76G)
0.0124
geranylgeranyl diphosphate
pH 8.5, 37°C, wild-type enzyme
0.0216
geranylgeranyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-A(wild-type)/subunit-B(V76G)
0.0478
geranylgeranyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-A(wild-type)/subunit-B(A79L)
0.385
geranylgeranyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-A(wild-type)/subunit-B(A79F)
0.0137
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-A(wild-type)/subunit-B(V76G)
0.0184
isopentenyl diphosphate
pH 8.5, 37°C, wild-type enzyme
0.0186
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-A(wild-type)/subunit-B(A79F)
0.0216
isopentenyl diphosphate
pH 8.5, 37°C, mutant enzyme subunit-A(wild-type)/subunit-B(A79L)
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A79F
mutant enzyme subunit-A(wild-type)/subunit-B(A79L) shows 10fold increased Vmax-values and 11fold decreased Km-values for geranyl diphosphate, which becomes the most preferred substrate of the allylic primers. 5fold increase in KM-value for geranylgeranyl diphosphate. Mutation results in shortening the chain length of the major product. The major products are farnesylgeranyl diphosphate and geranylgeranyl diphosphate
A79L
mutant enzyme subunit-A(wild-type)/subunit-B(A79L) shows 7fold increased Vmax-values and 6fold decreased Km-values for geranyl diphosphate, which becomes the most preferred substrate of the allylic primers. 3.9fold increase in KM-value for geranylgeranyl diphosphate. Mutation results in shortening the chain length of the major product. The major product is farnesylgeranyl diphosphate
V76G
mutant enzyme subunit-A(wild-type)/subunit-B(V76G) gives octaprenyl diphosphate as the final products with farnesyl diphosphate as an allylic primer
A79F
-
mutant enzyme subunit-A(wild-type)/subunit-B(A79L) shows 10fold increased Vmax-values and 11fold decreased Km-values for geranyl diphosphate, which becomes the most preferred substrate of the allylic primers. 5fold increase in KM-value for geranylgeranyl diphosphate. Mutation results in shortening the chain length of the major product. The major products are farnesylgeranyl diphosphate and geranylgeranyl diphosphate
-
A79L
-
mutant enzyme subunit-A(wild-type)/subunit-B(A79L) shows 7fold increased Vmax-values and 6fold decreased Km-values for geranyl diphosphate, which becomes the most preferred substrate of the allylic primers. 3.9fold increase in KM-value for geranylgeranyl diphosphate. Mutation results in shortening the chain length of the major product. The major product is farnesylgeranyl diphosphate
-
V76G
-
mutant enzyme subunit-A(wild-type)/subunit-B(V76G) gives octaprenyl diphosphate as the final products with farnesyl diphosphate as an allylic primer
-
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
-
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Fujii, H.; Koyama, T.; Ogura, K.
Hexaprenyl pyrophosphate synthetase from Micrococcus luteus B-P 26. Separation of two essential components
J. Biol. Chem.
257
14610-14612
1982
Micrococcus luteus (O66127 and O66129), Micrococcus luteus B-P 26 (O66127 and O66129), Micrococcus luteus B-P 26
brenda
Yoshida, I.; Koyama, T.; Ogura, K.
Formation of a stable and catalytically active complex of the two essential components of hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26
Biochem. Biophys. Res. Commun.
160
448-452
1989
Micrococcus luteus (O66127 and O66129), Micrococcus luteus B-P 26 (O66127 and O66129)
brenda
Yoshida, I.; Koyama, T.; Ogura, K.
Protection of hexaprenyl-diphosphate synthase of Micrococcus luteus B-P 26 against inactivation by sulphydryl reagents and arginine-specific reagents
Biochim. Biophys. Acta
995
138-143
1989
Micrococcus luteus (O66127 and O66129), Micrococcus luteus B-P 26 (O66127 and O66129)
brenda
Shimizu, N.; Koyama, T.; Ogura, K.
Molecular cloning, expression, and characterization of the genes encoding the two essential protein components of Micrococcus luteus B-P 26 hexaprenyl diphosphate synthase
J. Bacteriol.
180
1578-1581
1998
Micrococcus luteus (O66127 and O66129), Micrococcus luteus B-P 26 (O66127 and O66129)
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
Micrococcus luteus (O66127 and O66129), Micrococcus luteus B-P 26 (O66127 and O66129)
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
Micrococcus luteus (O66127 and O66129), Micrococcus luteus B-P 26 (O66127 and O66129)
brenda
Yoshida, I.; Koyama, T.; Ogura, K.
Dynamic Interaction between Components of Hexaprenyl Diphosphate Synthase from Micrococcus luteus BP-26
Biochemistry
26
6840-6845
1987
Micrococcus luteus (O66127 and O66129), Micrococcus luteus BP-26 (O66127 and O66129)
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
Micrococcus luteus (O66127 and O66129), Micrococcus luteus B-P 26 (O66127 and O66129)
brenda
Sasaki, D.; Fujihashi, M.; Okuyama, N.; Kobayashi, Y.; Noike, M.; Koyama, T.; Miki, K.
Crystal structure of heterodimeric hexaprenyl diphosphate synthase from Micrococcus luteus B-P 26 reveals that the small subunit is directly involved in the product chain length regulation
J. Biol. Chem.
286
3729-3740
2011
Micrococcus luteus (O66129 and O66127), Micrococcus luteus B-P 26 (O66129 and O66127)
brenda
Li, L.; Furubayashi, M.; Hosoi, T.; Seki, T.; Otani, Y.; Kawai-Noma, S.; Saito, K.; Umeno, D.
Construction of a nonnatural C60 carotenoid biosynthetic pathway
ACS Synth. Biol.
8
511-520
2019
Micrococcus luteus
brenda
Camesasca, L.; Minteguiaga, M.; Farina, L.; Salzman, V.; Aguilar, P.S.; Gaggero, C.; Carrau, F.
Overproduction of isoprenoids by Saccharomyces cerevisiae in a synthetic grape juice medium in the absence of plant genes
Int. J. Food Microbiol.
282
42-48
2018
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4743
brenda