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Information on EC 2.5.1.31 - ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific] and Organism(s) Micrococcus luteus and UniProt Accession O82827
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2.5.1.31 ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]IUBMB Comments
Undecaprenyl pyrophosphate synthase catalyses the consecutive condensation reactions of a farnesyl diphosphate with eight isopentenyl diphosphates, in which new cis-double bonds are formed, to generate undecaprenyl diphosphate that serves as a lipid carrier for peptidoglycan synthesis of bacterial cell wall .
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Word Map
- 2.5.1.31
-
isoprenoids
- cis-prenyltransferase
- prenyltransferases
- dolichols
- luteus
- dhdds
- trans-prenyltransferases
- pharmacology
-
octaprenyl
- drug development
- medicine
The taxonomic range for the selected organisms is: Micrococcus luteus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
undecaprenyl diphosphate synthase, undecaprenyl pyrophosphate synthase, dehydrodolichyl diphosphate synthase, upp synthase, ddpps, undecaprenyl pyrophosphate synthetase, upp synthetase, z-prenyl diphosphate synthase, undecaprenyl-diphosphate synthase, isosesquilavandulyl diphosphate synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
undecaprenyl diphosphate synthase
-
bactoprenyl-diphosphate synthase
-
-
-
-
C55-OO synthetase
-
-
-
-
C55PP synthetase
-
-
-
-
cis,polyprenyl diphosphate synthase
-
-
-
-
CPDS
-
-
-
-
DDPPs
-
-
-
-
dehydrodolichyl diphosphate synthase
-
-
-
-
di-trans,poly-cis-undecaprenyl-diphosphate synthase
-
-
-
-
synthetase, undecaprenyl pyrophosphate
-
-
-
-
undecaprenyl diphosphate synthase
undecaprenyl diphosphate synthetase
-
-
-
-
undecaprenyl pyrophosphate synthetase
-
-
-
-
undecaprenyl-diphosphate synthase
-
-
-
-
UPP synthetase
-
-
-
-
UPS
-
-
-
-
Z-prenyl diphosphate synthase
-
-
-
-
undecaprenyl diphosphate synthase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
catalytic mechanism, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alkenyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 8 isopentenyl units)
Undecaprenyl pyrophosphate synthase catalyses the consecutive condensation reactions of a farnesyl diphosphate with eight isopentenyl diphosphates, in which new cis-double bonds are formed, to generate undecaprenyl diphosphate that serves as a lipid carrier for peptidoglycan synthesis of bacterial cell wall [3].
CAS REGISTRY NUMBER
COMMENTARY
52350-87-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate
?
-
-
-
?
isopentenyl diphosphate + farnesyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
isopentenyl diphosphate + geranylgeranyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
-
-
-
-
?
(2Z,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate
?
-
-
-
-
?
di-trans-poly-cis-decaprenyl diphosphate + isopentenyl diphosphate
diphosphate + di-trans-poly-cis-undecaprenyl diphosphate
di-trans-poly-cis-decaprenyl diphosphate is farnesyl diphosphate, isopentenyl diphosphate binding mode determination
-
-
?
farnesyl diphosphate + isopentenyl diphosphate
diphosphate + di-trans-poly-cis-undecaprenyl diphosphate
sequential condensation of 8 molecules of isopentenyl diphosphate in the cis-configuration into farnesyl diphosphate to produce undecaprenyl diphosphate, indispensable for the biosynthesis of bacterial cell wall
-
-
?
isopentenyl diphosphate + farnesyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
isopentenyl diphosphate + geranyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
-
-
-
-
?
isopentenyl diphosphate + geranylgeranyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
isopentenyl diphosphate + neryl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
-
-
-
-
?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
-
-
-
?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
catalyzes the cis-prenyl chain elongation onto trans,trans-farnesyl diphosphate (FPP) to produce undecaprenyl diphosphate (UPP). The product undecaprenyl diphosphate is indispensable for the biosynthesis of bacterial cell walls
-
-
?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
catalyzes the sequential condensation of eight molecules of isopentenyl diphosphate (IPP) in the cis-configuration into farnesyl diphosphate (FPP) to produce undecaprenyl diphosphate (UPP), which is indispensable for the biosynthesis of the bacterial cell wall
-
-
?
(2Z,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate
?
-
-
-
?
(2Z,6E,10E)-geranylgeranyl diphosphate + isopentenyl diphosphate
?
-
-
-
?
isopentenyl diphosphate + farnesyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
-
-
-
?
isopentenyl diphosphate + farnesyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
-
-
?
isopentenyl diphosphate + farnesyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
-
-
-
?
isopentenyl diphosphate + farnesyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
-
-
-
-
?
isopentenyl diphosphate + farnesyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
(Z,E,E)-farnesyl diphosphate
E193Q, R197S, E201Q, R203S, D221A, and D226A show product distribution pattern similar to that of the wild-type enzyme, which produces C55 prenyl diphosphate as its major product as well as minor amounts of some intermediates having shorter prenyl chains and C60 product. The major products of the mutant enzymes S74A and E216Q contain C35 and C50 prenyl chain length. Mutant enzyme F73A produces a mixture of C30 and C35 products
?
isopentenyl diphosphate + geranylgeranyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
-
-
-
?
isopentenyl diphosphate + geranylgeranyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
(Z,E,E)-geranylgeranyl diphosphate
-
-
?
isopentenyl diphosphate + farnesyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
-
-
-
-
?
isopentenyl diphosphate + farnesyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
-
cis,trans-farnesyl diphosphate
-
-
?
isopentenyl diphosphate + farnesyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
(E,E)-farnesyl diphosphate
-
-
?
isopentenyl diphosphate + farnesyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
-
trans,trans-farnesyl diphosphate
-
-
?
isopentenyl diphosphate + farnesyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
trans,trans-farnesyl diphosphate
-
-
?
isopentenyl diphosphate + geranylgeranyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
-
-
-
-
?
isopentenyl diphosphate + geranylgeranyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
(Z,E,E)-geranylgeranyl diphosphate
-
-
?
isopentenyl diphosphate + geranylgeranyl diphosphate
C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate
-
trans,trans,trans-geranylgeranyl diphosphate and cis,trans,trans-geranylgeranyl diphosphate
-
-
?
additional information
?
-
-
catalyzes the sequential cis-condensation of isopentenyl diphosphate onto (2E,6E)-farnesyl diphosphate
-
-
?
additional information
?
-
catalyzes the sequential cis-condensation of isopentenyl diphosphate onto (2E,6E)-farnesyl diphosphate
-
-
?
additional information
?
-
-
reactivities of the allylic substrates increase with chain length: C10, C15, C20. Each new isoprene unit added has a cis-configuration
-
-
?
additional information
?
-
-
the product undecaprenyl diphosphate is indispensable for the biosynthesis of bacterial cell walls
-
-
?
additional information
?
-
the product undecaprenyl diphosphate is indispensable for the biosynthesis of bacterial cell walls
-
-
?
additional information
?
-
-
involved in the biosynthesis of long-chain polyprenyl diphosphate required as a carbohydrate carrier in the biosynthesis of a variety of bacterial cell envelope components
-
-
?
additional information
?
-
-
artificial substrate analogs, 3-desmethyl farnesyl diphosphate and 3-desmethyl Z-geranylgeranyl diphosphate are not used as substrates. The methyl group at the 3-position of the allylic substrate is important in the undecaprenyl diphosphate synthase reaction. The binding sites for the natural substrate farnesyl diphosphate and those for the intermediate allylic diphosphate, which contains the cis-prenyl unit, are different during the cis-prenyl chain elongation reaction
-
-
?
additional information
?
-
-
artificial substrate analogs, 3-desmethyl farnesyl diphosphate and 3-desmethyl (2Z,6E,10E)-geranylgeranyl diphosphate are not used as substrates. The methyl group at the 3-position of the allylic substrate is important in the undecaprenyl diphosphate synthase reaction. The binding sites for the natural substrate farnesyl diphosphate and those for the intermediate allylic diphosphate, which contains the cis-prenyl unit, are different during the cis-prenyl chain elongation reaction
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
-
-
-
-
?
farnesyl diphosphate + isopentenyl diphosphate
diphosphate + di-trans-poly-cis-undecaprenyl diphosphate
sequential condensation of 8 molecules of isopentenyl diphosphate in the cis-configuration into farnesyl diphosphate to produce undecaprenyl diphosphate, indispensable for the biosynthesis of bacterial cell wall
-
-
?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
catalyzes the cis-prenyl chain elongation onto trans,trans-farnesyl diphosphate (FPP) to produce undecaprenyl diphosphate (UPP). The product undecaprenyl diphosphate is indispensable for the biosynthesis of bacterial cell walls
-
-
?
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate
8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
catalyzes the sequential condensation of eight molecules of isopentenyl diphosphate (IPP) in the cis-configuration into farnesyl diphosphate (FPP) to produce undecaprenyl diphosphate (UPP), which is indispensable for the biosynthesis of the bacterial cell wall
-
-
?
additional information
?
-
-
catalyzes the sequential cis-condensation of isopentenyl diphosphate onto (2E,6E)-farnesyl diphosphate
-
-
?
additional information
?
-
catalyzes the sequential cis-condensation of isopentenyl diphosphate onto (2E,6E)-farnesyl diphosphate
-
-
?
additional information
?
-
-
the product undecaprenyl diphosphate is indispensable for the biosynthesis of bacterial cell walls
-
-
?
additional information
?
-
the product undecaprenyl diphosphate is indispensable for the biosynthesis of bacterial cell walls
-
-
?
additional information
?
-
-
involved in the biosynthesis of long-chain polyprenyl diphosphate required as a carbohydrate carrier in the biosynthesis of a variety of bacterial cell envelope components
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
divalent metal ion required, Mg2+ is most effective, optimal concentration is 240 nM
Co2+
Mg2+
Mn2+
-
enzyme is optimally stimulated by 0.1 mM Mg2+, 0.05 mM Mn2+ or 0.2 mM Co2+
Co2+
-
enzyme is optimally stimulated by 0.1 mM Mg2+, 0.05 mM Mn2+ or 0.2 mM Co2+
Mg2+
-
enzyme is optimally stimulated by 0.1 mM Mg2+, 0.05 mM Mn2+ or 0.2 mM Co2+
Mg2+
-
required, structures of Mg2+ binding of wild-type and mutant UPPS, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SO42-
competitive inhibitor with respect to (2E,6E)-farnesyl diphosphate
3-desmethyl (2Z,6E,10E)-geranylgeranyl diphosphate
-
mixed inhibition with farnesyl diphosphate, competitive inhibition with reaction intermediate (2Z,6E,10E)-geranylgeranyl diphosphate
3-desmethyl Z-geranylgeranyl diphosphate
-
mixed inhibition with farnesyl diphosphate, competitive inhibition with reaction intermediate (Z,E,E)-geranylgeranyl diphosphate
tetramic acid
-
the crystal structure is used for modelling with bound inhibitor tetramic acid
Triton X-100
-
marked decrease of activity when a small amount of detergent is added, activity gradually increases as further detergent is added, being fully restored when the concentration reaches 2%
3-desmethyl farnesyl diphosphate
-
competitive with farnesyl diphosphate, mixed inhibition with reaction intermediate (Z,E,E)-geranylgeranyl diphosphate
3-desmethyl farnesyl diphosphate
-
competitive with farnesyl diphosphate, mixed inhibition with reaction intermediate (2Z,6E,10E)-geranylgeranyl diphosphate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
lysophosphatidylglycerol
-
weak effect in activating lipid-depleted enzyme
additional information
-
enzyme is inactive in absence of added effectors
-
Triton X-100
-
marked decrease of activity when a small amount of detergent is added, activity gradually increases as further detergent is added, being fully restored when the concentration reaches 2%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0075
geranylgeranyl diphosphate
mutant enzyme D226A, pH 7.3, 37°C
0.0104
(2E,6E)-farnesyl diphosphate
mutant enzyme N77Q, pH 7.5, 37°C
0.0139
(2E,6E)-farnesyl diphosphate
mutant enzyme N77D, pH 7.5, 37°C
0.0147
(2E,6E)-farnesyl diphosphate
mutant enzyme N77A, pH 7.5, 37°C
0.0495
(2E,6E)-farnesyl diphosphate
mutant enzyme W78I, pH 7.5, 37°C
0.1207
(2E,6E)-farnesyl diphosphate
mutant enzyme W78R, pH 7.5, 37°C
0.155
(2E,6E)-farnesyl diphosphate
mutant enzyme N78D, pH 7.5, 37°C
0.0088
(2E,6E,10E)-geranylgeranyl diphosphate
wild-type, pH 7.5, 37°C
0.064
(2E,6E,10E)-geranylgeranyl diphosphate
R33A mutant, pH 7.5, 37°C
0.0043
(2Z,6E,10E)-geranylgeranyl diphosphate
G32R mutant, pH 7.5, 37°C
0.0045
(2Z,6E,10E)-geranylgeranyl diphosphate
R42G mutant, pH 7.5, 37°C
0.005
(2Z,6E,10E)-geranylgeranyl diphosphate
mutant enzyme N77Q, pH 7.5, 37°C
0.005
(2Z,6E,10E)-geranylgeranyl diphosphate
D29A mutant, pH 7.5, 37°C
0.0059
(2Z,6E,10E)-geranylgeranyl diphosphate
G32R-R42G mutant, pH 7.5, 37°C
0.006
(2Z,6E,10E)-geranylgeranyl diphosphate
E84Q mutant, pH 7.5, 37°C
0.0061
(2Z,6E,10E)-geranylgeranyl diphosphate
R80A mutant, pH 7.5, 37°C
0.008
(2Z,6E,10E)-geranylgeranyl diphosphate
mutant enzyme N77D, pH 7.5, 37°C; mutant enzyme W78D, pH 7.5, 37°C
0.0082
(2Z,6E,10E)-geranylgeranyl diphosphate
wild-type enzyme, pH 7.5, 37°C
0.0082
(2Z,6E,10E)-geranylgeranyl diphosphate
wild-type, pH 7.5, 37°C
0.0095
(2Z,6E,10E)-geranylgeranyl diphosphate
R33A mutant, pH 7.5, 37°C
0.0102
(2Z,6E,10E)-geranylgeranyl diphosphate
mutant enzyme N77A, pH 7.5, 37°C
0.015
(2Z,6E,10E)-geranylgeranyl diphosphate
mutant enzyme W78R, pH 7.5, 37°C
0.019
(2Z,6E,10E)-geranylgeranyl diphosphate
mutant enzyme W78I, pH 7.5, 37°C
0.023
(2Z,6E,10E)-geranylgeranyl diphosphate
E76Q mutant, pH 7.5, 37°C
5.3
(2Z,6E,10E)-geranylgeranyl diphosphate
S74A mutant, pH 7.3, 37°C
5.8
(2Z,6E,10E)-geranylgeranyl diphosphate
E216Q mutant, pH 7.3, 37°C
6
(2Z,6E,10E)-geranylgeranyl diphosphate
R197S mutant, pH 7.3, 37°C
7.5
(2Z,6E,10E)-geranylgeranyl diphosphate
D226A mutant, pH 7.3, 37°C
8.1
(2Z,6E,10E)-geranylgeranyl diphosphate
E193Q mutant, pH 7.3, 37°C
8.1
(2Z,6E,10E)-geranylgeranyl diphosphate
R203S mutant, pH 7.3, 37°C
9.4
(2Z,6E,10E)-geranylgeranyl diphosphate
F73A mutant, pH 7.3, 37°C
17.7
(2Z,6E,10E)-geranylgeranyl diphosphate
E201Q mutant, pH 7.3, 37°C
18.1
(2Z,6E,10E)-geranylgeranyl diphosphate
D221A mutant, pH 7.3, 37°C
0.005
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme N77Q, pH 7.5, 37°C
0.0053
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme S74A, pH 7.3, 37°C
0.0058
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme R216Q, pH 7.3, 37°C
0.006
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme R197S, pH 7.3, 37°C
0.008
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme N77D, pH 7.5, 37°C
0.008
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme W78D, pH 7.5, 37°C
0.0081
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme E193Q, pH 7.3, 37°C
0.0081
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme R203S, pH 7.3, 37°C
0.0082
(Z,E,E)-Geranylgeranyl diphosphate
wild-type enzyme, pH 7.5, 37°C
0.0082
(Z,E,E)-Geranylgeranyl diphosphate
wild-type enzyme, pH 7.3, 37°C
0.0094
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme F73A, pH 7.3, 37°C
0.0102
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme N77A, pH 7.5, 37°C
0.015
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme W78R, pH 7.5, 37°C
0.0177
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme E201Q, pH 7.3, 37°C
0.0181
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme D221A, pH 7.3, 37°C
0.019
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme W78I, pH 7.5, 37°C
0.0023
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme E76Q, pH 7.5, 37°C
0.0043
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme G32R, pH 7.5, 37°C
0.0045
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme R42G, pH 7.5, 37°C
0.005
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme D29A, pH 7.5, 37°C
0.0059
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme G32R/R42G, pH 7.5, 37°C
0.006
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme E84Q, pH 7.5, 37°C
0.0061
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme R80A, pH 7.5, 37°C
0.0082
(Z,E,E)-Geranylgeranyl diphosphate
wild-type enzyme, pH 7.5, 37°C
0.0095
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme R33A, pH 7.5, 37°C
0.0083
farnesyl diphosphate
pH 7.5, 30°C, recombinant wild-type enzyme
0.0059
isopentenyl diphosphate
mutant enzyme G32R/R42G, pH 7.5, 37°C
0.0078
isopentenyl diphosphate
pH 7.5, 30°C, recombinant wild-type enzyme
0.018
isopentenyl diphosphate
pH 7.5, 30°C, recombinant mutant W210A
0.023
isopentenyl diphosphate
pH 7.5, 30°C, recombinant mutant Y148F
0.026
isopentenyl diphosphate
pH 7.5, 30°C, recombinant mutant Y71S
0.036
isopentenyl diphosphate
pH 7.5, 30°C, recombinant mutant Y148F
0.103
isopentenyl diphosphate
pH 7.5, 30°C, recombinant mutant F207S
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00125
(2E,6E)-farnesyl diphosphate
mutant enzyme N77A, pH 7.5, 37°C
0.00155
(2E,6E)-farnesyl diphosphate
mutant enzyme N77Q, pH 7.5, 37°C
0.00272
(2E,6E)-farnesyl diphosphate
mutant enzyme N77D, pH 7.5, 37°C
0.151
(2E,6E)-farnesyl diphosphate
mutant enzyme W78D, pH 7.5, 37°C
0.434
(2E,6E)-farnesyl diphosphate
mutant enzyme N78R, pH 7.5, 37°C
0.456
(2E,6E)-farnesyl diphosphate
mutant enzyme W78I, pH 7.5, 37°C
0.002
(2Z,6E,10E)-geranylgeranyl diphosphate
mutant enzyme N77A, pH 7.5, 37°C
0.00231
(2Z,6E,10E)-geranylgeranyl diphosphate
mutant enzyme N77Q, pH 7.5, 37°C
0.00415
(2Z,6E,10E)-geranylgeranyl diphosphate
mutant enzyme N77D, pH 7.5, 37°C
0.00579
(2Z,6E,10E)-geranylgeranyl diphosphate
R80A mutant, pH 7.5, 37°C
0.0258
(2Z,6E,10E)-geranylgeranyl diphosphate
D29A mutant, pH 7.5, 37°C
0.0813
(2Z,6E,10E)-geranylgeranyl diphosphate
R33A mutant, pH 7.5, 37°C
0.3
(2Z,6E,10E)-geranylgeranyl diphosphate
mutant enzyme W78D, pH 7.5, 37°C
0.382
(2Z,6E,10E)-geranylgeranyl diphosphate
R42G mutant, pH 7.5, 37°C
0.604
(2Z,6E,10E)-geranylgeranyl diphosphate
E76Q mutant, pH 7.5, 37°C
0.608
(2Z,6E,10E)-geranylgeranyl diphosphate
G32R mutant, pH 7.5, 37°C
0.899
(2Z,6E,10E)-geranylgeranyl diphosphate
mutant enzyme W78R, pH 7.5, 37°C
1.07
(2Z,6E,10E)-geranylgeranyl diphosphate
E84Q mutant, pH 7.5, 37°C
1.11
(2Z,6E,10E)-geranylgeranyl diphosphate
G32R/R42G mutant, pH 7.5, 37°C
1.37
(2Z,6E,10E)-geranylgeranyl diphosphate
mutant enzyme W78I, pH 7.5, 37°C
1.77
(2Z,6E,10E)-geranylgeranyl diphosphate
wild-type enzyme, pH 7.5, 37°C
1.77
(2Z,6E,10E)-geranylgeranyl diphosphate
wild-type, pH 7.5, 37°C
0.002
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme N77A, pH 7.5, 37°C
0.00231
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme N77Q, pH 7.5, 37°C
0.00415
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme N77D, pH 7.5, 37°C
0.3
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme W78D, pH 7.5, 37°C
0.899
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme W78R, pH 7.5, 37°C
1.37
(Z,E,E)-Geranylgeranyl diphosphate
mutant enzyme W78I, pH 7.5, 37°C
1.77
(Z,E,E)-Geranylgeranyl diphosphate
wild-type enzyme, pH 7.5, 37°C
1.22
farnesyl diphosphate
pH 7.5, 30°C, recombinant wild-type enzyme
0.002
isopentenyl diphosphate
pH 7.5, 30°C, recombinant mutant W210A
0.01
isopentenyl diphosphate
pH 7.5, 30°C, recombinant mutant F207S
0.071
isopentenyl diphosphate
pH 7.5, 30°C, recombinant mutant Y148F
0.115
isopentenyl diphosphate
pH 7.5, 30°C, recombinant mutant Y148F
1.55
isopentenyl diphosphate
pH 7.5, 30°C, recombinant wild-type enzyme
additional information
additional information
-
turnover number for recombinant wild-type enzyme and mutant enzymes Y71S, Y148F, F207S, W210A, W224A
-
additional information
additional information
turnover number for recombinant wild-type enzyme and mutant enzymes Y71S, Y148F, F207S, W210A, W224A
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.949
(2Z,6E,10E)-geranylgeranyl diphosphate
R80A mutant, pH 7.5, 37°C
5.2
(2Z,6E,10E)-geranylgeranyl diphosphate
D29A mutant, pH 7.5, 37°C
8.65
(2Z,6E,10E)-geranylgeranyl diphosphate
R33A mutant, pH 7.5, 37°C
26.3
(2Z,6E,10E)-geranylgeranyl diphosphate
E76Q mutant, pH 7.5, 37°C
84.8
(2Z,6E,10E)-geranylgeranyl diphosphate
R42G mutant, pH 7.5, 37°C
141
(2Z,6E,10E)-geranylgeranyl diphosphate
G32R mutant, pH 7.5, 37°C
178
(2Z,6E,10E)-geranylgeranyl diphosphate
E84Q mutant, pH 7.5, 37°C
188
(2Z,6E,10E)-geranylgeranyl diphosphate
G32R/R42G mutant, pH 7.5, 37°C
215.9
(2Z,6E,10E)-geranylgeranyl diphosphate
wild-type, pH 7.5, 37°C
additional information
additional information
-
kcat/KM-values for recombinant wild-type enzyme and mutant enzymes Y71S, Y148F, F207S, W210A, W224A
-
additional information
additional information
kcat/KM-values for recombinant wild-type enzyme and mutant enzymes Y71S, Y148F, F207S, W210A, W224A
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.017
3-desmethyl (2Z,6E,10E)-geranylgeranyl diphosphate
-
substrate farnesyl diphosphate, pH 7.5, 37°C
0.028
3-desmethyl (2Z,6E,10E)-geranylgeranyl diphosphate
-
substrate (Z,E,E)-geranylgeranyl diphosphate, pH 7.5, 37°C
0.045
3-desmethyl farnesyl diphosphate
-
substrate farnesyl diphosphate, pH 7.5, 37°C
2.8
3-desmethyl farnesyl diphosphate
-
substrate (Z,E,E)-geranylgeranyl diphosphate, pH 7.5, 37°C
2.8
3-desmethyl farnesyl diphosphate
-
substrate (2Z,6E,10E)-geranylgeranyl diphosphate, pH 7.5, 37°C
0.017
3-desmethyl Z-geranylgeranyl diphosphate
-
substrate farnesyl diphosphate, pH 7.5, 37°C
0.028
3-desmethyl Z-geranylgeranyl diphosphate
-
substrate (Z,E,E)-geranylgeranyl diphosphate, pH 7.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.534
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapour-diffusion method with ammonium sulfate and lithium sulfate as precipitants
the overall structure is determined at 2.2 A resolution by multiple isomorphous replacement with anomalous scattering
the crystal structure is used for moelling with bound inhibitor tetramic acid
-
the overall structure is determined at 2.2 A resolution by multiple isomorphous replacement with anomalous scattering
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A72L/F73L
mutation results in shorter ultimate products with C20-35
A72L/F73L/W78L
mutation results in shorter ultimate products with C20-35
D221A
comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. Km-value for isopentenyl diphosphate within moderate folds to that of the wild-type and slightly decreased enzymatic activity
D226A
comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. Km-value for isopentenyl diphosphate within moderate folds to that of the wild-type and slightly decreased enzymatic activity
D29A
Km-value for farnesyl diphosphate is 9.2fold higher than that for the wild-type enzyme. Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate is 1.6fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 5.8fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 1% of that of the wild-type enzyme
E193Q
comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. Km-value for isopentenyl diphosphate within moderate folds to that of the wild-type and slightly decreased enzymatic activity
E201Q
comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. Km-value for isopentenyl diphosphate within moderate folds to that of the wild-type and slightly decreased enzymatic activity
E216Q
E76Q
Km-value for farnesyl diphosphate is 1.6fold higher than that for the wild-type enzyme. Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate is 3.6fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 1.5fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 30% of that of the wild-type enzyme
E84Q
Km-value for farnesyl diphosphate is 3.2fold higher than that for the wild-type enzyme. Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate is 1.3fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 3.98fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 65% of that of the wild-type enzyme
F207S
site-directed mutagenesis, reduced activity, and 13fold increased Km for isopentenyl diphosphate compared to the wild-type enzyme
F223H
dramatically decreased catalytic activity when farnesyl diphosphate is used as allylic substrate
F73A
G32R
Km-value for farnesyl diphosphate is comparable to that of the wild-type enzyme. Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate is 1.9fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is comparable to that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 27% of that of the wild-type enzyme
G32R/R42G
Km-value for farnesyl diphosphate is 1.4fold higher than that for the wild-type enzyme. Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate is 1.4fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 1.3fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 58% of that of the wild-type enzyme
N77A
dramatic decrease in catalytic activity, but Km-values for both allylic and homoallylic substrates are comparable to those of the wild-type
N77D
dramatic decrease in catalytic activity, but Km-values for both allylic and homoallylic substrates are comparable to those of the wild-type
N77Q
dramatic decrease in catalytic activity, but Km-values for both allylic and homoallylic substrates are comparable to those of the wild-type
R197S
R203S
R33A
Km-value for farnesyl diphosphate is 40fold higher than that for the wild-type enzyme. Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate is 1.2fold lower than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 3% of that of the wild-type enzyme. Different product distribution pattern compared to the wildf-type enzyme
R42G
Km-value for farnesyl diphosphate is 1.4fold higher than that for the wild-type enzyme. Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate is 1.8fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 3.1fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 13% of that of the wild-type enzyme
R80A
Km-value for farnesyl diphosphate is 6.4fold higher than that for the wild-type enzyme. Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate is 1.3fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 6.3fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is less than 1% of that of the wild-type enzyme
S74A
W210A
site-directed mutagenesis, reduced activity, unaltered Km for both substrates compared to the wild-type enzyme
W224A
site-directed mutagenesis, reduced activity, 6fold increased Km for farnesyl diphosphate, and 14fold increased Km for isopentenyl diphosphate compared to the wild-type enzyme
W78D
moderate levels of enzymatic activity and comparable Km-values for isopentenyl diphosphate to that of the wild-type. 18.7fold increase in Km-value for farnesyl diphosphate
W78I
W78R
Y148F
site-directed mutagenesis, reduced activity, unaltered Km for both substrates compared to the wild-type enzyme
Y71S
site-directed mutagenesis, reduced activity, unaltered Km for both substrates compared to the wild-type enzyme
D29A
Km-value for farnesyl diphosphate is 9.2fold higher than that for the wild-type enzyme. Km-value for (Z,E,E)-geranylgeranyl diphosphate is 1.6fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 5.8fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 1% of that of the wild-type enzyme
E76Q
Km-value for farnesyl diphosphate is 1.6fold higher than that for the wild-type enzyme. Km-value for (Z,E,E)-geranylgeranyl diphosphate is 3.6fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 1.5fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 30% of that of the wild-type enzyme
E84Q
Km-value for farnesyl diphosphate is 3.2fold higher than that for the wild-type enzyme. Km-value for (Z,E,E)-geranylgeranyl diphosphate is 1.3fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 3.98fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 65% of that of the wild-type enzyme
F207S
site-directed mutagenesis, reduced activity, and 13fold increased Km for isopentenyl diphosphate compared to the wild-type enzyme
G32R
Km-value for farnesyl diphosphate is comparable to that of the wild-type enzyme. Km-value for (Z,E,E)-geranylgeranyl diphosphate is 1.9fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is comparable to that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 27% of that of the wild-type enzyme
G32R/R42G
Km-value for farnesyl diphosphate is 1.4fold higher than that for the wild-type enzyme. Km-value for (Z,E,E)-geranylgeranyl diphosphate is 1.4fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 1.3fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 58% of that of the wild-type enzyme
R33A
Km-value for farnesyl diphosphate is 40fold higher than that for the wild-type enzyme. Km-value for (Z,E,E)-geranylgeranyl diphosphate is 1.2fold lower than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 3% of that of the wild-type enzyme. Different product distribution pattern compared to the wildf-type enzyme
R42G
Km-value for farnesyl diphosphate is 1.4fold higher than that for the wild-type enzyme. Km-value for (Z,E,E)-geranylgeranyl diphosphate is 1.8fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 3.1fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is 13% of that of the wild-type enzyme
R80A
Km-value for farnesyl diphosphate is 6.4fold higher than that for the wild-type enzyme. Km-value for (Z,E,E)-geranylgeranyl diphosphate is 1.3fold lower than that of the wild-type enzyme. Km-value for isopentenyl diphosphate is 6.3fold higher than that of the wild-type enzyme. The turnover-number for farnesyl diphosphate is less than 1% of that of the wild-type enzyme
W210A
site-directed mutagenesis, reduced activity, unaltered Km for both substrates compared to the wild-type enzyme
W224A
site-directed mutagenesis, reduced activity, 6fold increased Km for farnesyl diphosphate, and 14fold increased Km for isopentenyl diphosphate compared to the wild-type enzyme
Y148F
site-directed mutagenesis, reduced activity, unaltered Km for both substrates compared to the wild-type enzyme
Y71S
site-directed mutagenesis, reduced activity, unaltered Km for both substrates compared to the wild-type enzyme
E216Q
comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. Km-value for isopentenyl diphosphate is about 11.6fold higher than that for the wild-type enzyme, turnover number is about 18fold lower. The major products contain C35 and C50 prenyl chain length
F73A
comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. 32fold increase in Km-value for isopentenyl diphosphate and about 17fold decrease in turnover-number. A mixture of C30 and C50 products is formed
F73A
yielded shorter chain prenyl diphosphates as their main products
R197S
comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. Km-value for isopentenyl diphosphate is about 7.2fold higher than that for the wild-type enzyme, turnover-number is 1200fold lower. Compared with the wild-type enzyme lower reaction rate in catalysis and fewer product produced after 6 h reaction
R203S
comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. Km-value for isopentenyl diphosphate is about 8fold higher than that for the wild-type enzyme, turnover-number is 1200fold lower. Compared with the wild-type enzyme lower reaction rate in catalysis and fewer product produced after 6 h reaction
S74A
comparable Km-values for farnesyl diphosphate and geranylgeranyl diphosphate with those of the wild-type enzyme. 16fold increase in Km-value for isopentenyl diphosphate and about 12fold decrease in turnover-number. The major products contain C35 and C50 prenyl chain length
S74A
yielded shorter chain prenyl diphosphates as their main products
W78I
moderate levels of enzymatic activity and comparable Km-values for isopentenyl diphosphate to that of the wild-type. 6-fold increase in Km-value for farnesyl diphosphate, 2.3fold increase in Km-value for (Z,E,E)-geranylgeranyl diphosphate
W78I
moderate levels of enzymatic activity and comparable Km-values for isopentenyl diphosphate to that of the wild-type. 6-fold increase in Km-value for farnesyl diphosphate, 2.3fold increase in Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate
W78R
moderate levels of enzymatic activity and comparable Km-values for isopentenyl diphosphate to that of the wild-type. 14.5-fold increase in Km-value for farnesyl diphosphate, 1.8fold increase in Km-value for (Z,E,E)-geranylgeranyl diphosphate
W78R
moderate levels of enzymatic activity and comparable Km-values for isopentenyl diphosphate to that of the wild-type. 14.5-fold increase in Km-value for farnesyl diphosphate, 1.8fold increase in Km-value for (2Z,6E,10E)-geranylgeranyl diphosphate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli, no sequence similarity between E-prenyl diphosphate and Z-prenyl diphosphate synthases
expression of mutant enzymes R197S, R203S and E216Q in Escherichia coli
overexpression of wild-type and mutant enzymes in Escherichia coli strain JM109
overexpression of wild-type and mutant enzymes in Escherichia coli strain JM109
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Allen, C.M.
Purification and characterization of undecaprenylpyrophosphate synthetase
Methods Enzymol.
110
281-299
1985
Bacillus subtilis, Lactiplantibacillus plantarum, Micrococcus luteus, Salmonella newington
Koyama, T.; Yoshida, I.; Ogura, K.
Undecaprenyl diphosphate synthase from Micrococcus luteus B-P 26: essential factors for the enzymatic activity
J. Biochem.
103
867-871
1988
Micrococcus luteus, Micrococcus luteus B-P 26
Baba, T.; Allen, C.M.
Prenyl transferases from Micrococcus luteus: characterization of undecaprenyl pyrophosphate synthetase
Arch. Biochem. Biophys.
200
474-484
1980
Micrococcus luteus
Fujikura, K.; Zhang, Y.W.; Yoshizaki, H.; Nishino, T.; Koyama, T.
Significance of Asn-77 and Trp-78 in the catalytic function of undecaprenyl diphosphate synthase of Micrococcus luteus B-P 26
J. Biochem.
128
917-922
2000
Micrococcus luteus (O82827), Micrococcus luteus B-P 26 (O82827), Micrococcus luteus B-P 26
Shimizu, N.; Koyama, T.; Ogura, K.
Molecular cloning, expression, and purification of undecaprenyl diphosphate synthase. No sequence similarity between E- and Z-prenyl diphosphate synthases
J. Biol. Chem.
273
19476-19481
1998
Escherichia coli, Micrococcus luteus (O82827), Micrococcus luteus B-P 26 (O82827), Micrococcus luteus B-P 26
Fujihashi, M.; Zhang, Y.W.; Higuchi, Y.; Li, X.Y.; Koyama, T.; Miki, K.
Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase
Proc. Natl. Acad. Sci. USA
98
4337-4342
2001
Micrococcus luteus, Micrococcus luteus (O82827), Micrococcus luteus B-P 26, Micrococcus luteus B-P 26 (O82827)
Kharel, Y.; Zhang, Y.W.; Fujihashi, M.; Miki, K.; Koyama, T.
Identification of significant residues for homoallylic substrate binding of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase
J. Biol. Chem.
276
28459-28464
2001
Micrococcus luteus (O82827), Micrococcus luteus B-P 26 (O82827), Micrococcus luteus B-P 26
Fujikura, K.; Zhang, Y.W.; Fujihashi, M.; Miki, K.; Koyama, T.
Mutational analysis of allylic substrate binding site of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase
Biochemistry
42
4035-4041
2003
Micrococcus luteus, Micrococcus luteus (O82827), Micrococcus luteus B-P 26, Micrococcus luteus B-P 26 (O82827)
Khare, Y.; Zhang, Y.W.; Fujihashi, M.; Miki, K.; Koyama, T.
Significance of highly conserved aromatic residues in Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase
J. Biochem.
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Micrococcus luteus, Micrococcus luteus (O82827), Micrococcus luteus B-P 26, Micrococcus luteus B-P 26 (O82827)
Takahashi, S.; Koyama, T.
Structure and function of cis-prenyl chain elongating enzymes
Chem. Rec.
6
194-205
2006
Escherichia coli, Micrococcus luteus (O82827), Micrococcus luteus B-P 26 (O82827), Micrococcus luteus B-P 26
Kharel, Y.; Takahashi, S.; Yamashita, S.; Koyama, T.
Manipulation of prenyl chain length determination mechanism of cis-prenyltransferases
FEBS J.
273
647-657
2006
Micrococcus luteus (O82827), Micrococcus luteus, Micrococcus luteus B-P 26 (O82827), Micrococcus luteus B-P 26
Fujikura, K.; Maki, Y.; Ohya, N.; Satoh, M.; Koyama, T.
Kinetic studies of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase reaction using 3-desmethyl allylic substrate analogs
Biosci. Biotechnol. Biochem.
72
851-855
2008
Micrococcus luteus, Micrococcus luteus B-P 26
Fujihashi, M.; Shimizu, N.; Zhang, Y.W.; Koyama, T.; Miki, K.
Crystallization and preliminary X-ray diffraction studies of undecaprenyl diphosphate synthase from Micrococcus luteus B-P 26
Acta Crystallogr. Sect. D
55
1606-1607
1999
Micrococcus luteus (O82827), Micrococcus luteus B-P 26 (O82827), Micrococcus luteus B-P 26
Teng, K.; Liang, P.
Structures, mechanisms and inhibitors of undecaprenyl diphosphate synthase: A cis-prenyltransferase for bacterial peptidoglycan biosynthesis
Bioorg. Chem.
43
51-57
2012
Escherichia coli, Micrococcus luteus, Micrococcus luteus B-P 26, Streptococcus pneumoniae (Q97SR4)
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