2.5.1.31: ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
This is an abbreviated version!
For detailed information about ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific], go to the full flat file.
Word Map on EC 2.5.1.31
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2.5.1.31
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isoprenoids
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cis-prenyltransferase
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prenyltransferases
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dolichols
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luteus
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dhdds
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trans-prenyltransferases
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pharmacology
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octaprenyl
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drug development
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medicine
- 2.5.1.31
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isoprenoids
- cis-prenyltransferase
- prenyltransferases
- dolichols
- luteus
- dhdds
- trans-prenyltransferases
- pharmacology
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octaprenyl
- drug development
- medicine
Reaction
Synonyms
bactoprenyl-diphosphate synthase, C55-OO synthetase, C55PP synthetase, cis,polyprenyl diphosphate synthase, cis-prenyl chain elongating enzyme, cis-type undecaprenyl pyrophosphate synthase, CPDS, DDPPs, dehydrodolichyl diphosphate synthase, di-trans,poly-cis-decaprenylcistransferase, di-trans,poly-cis-undecaprenyl-diphosphate synthase, di-trans-poly-cis-decaprenyl cistransferase, isosesquilavandulyl diphosphate synthase, Mcl22, More, synthetase, undecaprenyl pyrophosphate, undecaprenyl diphosphate phosphatase, undecaprenyl diphosphate synthase, undecaprenyl diphosphate synthetase, undecaprenyl pyrophosphate synthase, undecaprenyl pyrophosphate synthetase, undecaprenyl-diphosphate synthase, undecaprenyl-pyrophosphate synthase, UPP synthase, UPP synthetase, UPP, C55 synthase, UPPs, UPS, Z-prenyl diphosphate synthase
ECTree
2.5.1.31 ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]Advanced search results
results (
results (Engineering
Engineering on EC 2.5.1.31 - ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
T86I
A143V
the C30 intermediate is formed to a greater extent and is longer lived in the process catalyzed by the A69L mutant
A69L
the small side chain of Ala-69 is required for rapid elongation to the C55 product
D150A
D218A
-
turnover-number is about 9% of the activity of the wild-type enzyme, Km value for farnesyl diphosphate is equal to that of the wild-type enzyme, Km-value for isopentenyl diphosphate is comparable to that of the wild-type enzyme
D26A
D26E
site-directed mutagenesis, altered Mg2+ binding and over 10000fold reduced activity compared to the wild-type enzyme
D26K
site-directed mutagenesis, altered Mg2+ binding and about 10000fold reduced activity compared to the wild-type enzyme
D26R
site-directed mutagenesis, altered Mg2+ binding and over 10000fold reduced activity compared to the wild-type enzyme
DELTAS72
-
loop-shortening mutant. Change of the length of the loop 72-83 impairs the ability of conformational change and causes remarkably lower activity of UPPs
DELTAS83
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loop-shortening mutant. Change of the length of the loop 72-83 impairs the ability of conformational change and causes remarkably lower activity of UPPs
DELTAV82S83
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loop-shortening mutant. Change of the length of the loop 72-83 impairs the ability of conformational change and causes remarkably lower activity of UPPs
E213A
E73A
E81A
F89A
H103A
the product distributions formed by the use of the I62A, V105A, and H103A mutants are similar to those observed for wild-type UPPs
H199A
-
site-directed mutagenesis, activity is similar to the wild-type enzyme
H199A/E213A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
H43A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
I62A
the product distributions formed by the use of the I62A, V105A, and H103A mutants are similar to those observed for wild-type UPPs
L137A
L85A
L88A
N74A
R77A
S71A
V105A
the product distributions formed by the use of the I62A, V105A, and H103A mutants are similar to those observed for wild-type UPPs
W149F
-
turnover-number is 68% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is 1.75fold higher than that of the wild-type enzyme, Km-value for isopentenyl diphosphate is 4.9fold higher than that of the wild-type enzyme
W207F
-
turnover-number is 60% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is 8.5fold higher than that of the wild-type enzyme, Km-value for isopentenyl diphosphate is 5.6fold higher than that of the wild-type enzyme
W221F
-
turnover-number is 140% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is 1.3fold higher than that of the wild-type enzyme, Km-value for isopentenyl diphosphate is 3.4fold higher than that of the wild-type enzyme
W31F
-
turnover-number is 44% of that of the wild-type enzyme,Km-value for farnesyl diphosphate is 5fold higher than that of the wild-type enzyme, Km-value for isopentenyl diphosphate is 1.4fold higher than that of the wild-type enzyme
W75A
W75F
-
turnover-number is 44% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is 4.5fold higher than that of the wild-type enzyme, Km-value for isopentenyl diphosphate is 6.3fold higher than that of the wild-type enzyme
W91F
-
turnover-number is equal to that of the wild-type enzyme, Km-value for farnesyl diphosphate is equal to that of the wild-type enzyme, Km-value for isopentenyl diphosphate is 1.8fold higher than that of the wild-type enzyme
C234A
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
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
E84Q
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
G32R/R42G
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
R42G
R80A
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
A72L/F73L/W78L
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mutation results in shorter ultimate products with C20-35
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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
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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
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D29A
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
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E76Q
E84Q
F207S
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site-directed mutagenesis, reduced activity, and 13fold increased Km for isopentenyl diphosphate compared to the wild-type enzyme
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G32R
G32R/R42G
N77A
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dramatic decrease in catalytic activity, but Km-values for both allylic and homoallylic substrates are comparable to those of the wild-type
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N77D
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dramatic decrease in catalytic activity, but Km-values for both allylic and homoallylic substrates are comparable to those of the wild-type
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N77Q
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dramatic decrease in catalytic activity, but Km-values for both allylic and homoallylic substrates are comparable to those of the wild-type
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S74A
W210A
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site-directed mutagenesis, reduced activity, unaltered Km for both substrates compared to the wild-type enzyme
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W78D
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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
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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
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Y148F
-
site-directed mutagenesis, reduced activity, unaltered Km for both substrates compared to the wild-type enzyme
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Y71S
-
site-directed mutagenesis, reduced activity, unaltered Km for both substrates compared to the wild-type enzyme
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additional information
T86I
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construction of strain TI392, with resistance to bacitracin, from strain YO-005, which is also modified with the mutation from strain SC26, conferring resistance to scandium, in Bacillus subtilis mutants
T86I
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construction of strain TI392, with resistance to bacitracin, from strain YO-005, which is also modified with the mutation from strain SC26, conferring resistance to scandium, in Bacillus subtilis mutants
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D150A
-
turnover-number is 44% of the activity of the wild-type enzyme, Km value for farnesyl diphosphate is equal to that of the wild-type enzyme, Km-value for isopentenyl diphosphate is about 50fold higher than that of the wild-type enzyme
D150A
-
turnover-number is 44% of the activity of the wild-type enzyme, Km value for (2E,6E)-farnesyl diphosphate is equal to that of the wild-type enzyme, Km-value for isopentenyl diphosphate is about 50fold higher than that of the wild-type enzyme
D26A
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turnover-number is less than 1% of that of the wild-type enzyme, Km value for farnesyl diphosphate is comparable to that of the wild-type enzyme, Km-value for isopentenyl diphosphate is 3.5fold higher than that of the wild-type enzyme
D26A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D26A
site-directed mutagenesis, altered Mg2+ binding and about 1000fold reduced activity compared to the wild-type enzyme
D26A
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the mutant shows altered Mg2+ binding compared to the wild-type enzyme
E213A
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turnover-number is less than 1% of the activity of the wild-type enzyme, Km value for farnesyl diphosphate is 1.75fold higher than that of the wild-type enzyme, Km-value for isopentenyl diphosphate is about 68.3fold higher than that of the wild-type enzyme
E213A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
E73A
-
turnover-number is 12% of that of the wild-type enzyme, Km value for farnesyl diphosphate is equal to that of the wild-type enzyme, Km-value for isopentenyl diphosphate is about 4fold higher than that of the wild-type enzyme
E73A
turnover-number is 12% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is equal to that of the wild-type enzyme, the Km-value for isopentenyl diphosphate is 3.9fold higher than that of the wild-type enzyme
E81A
turnover-number is 16% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is equal to that of the wild-type enzyme, the Km-value for isopentenyl diphosphate is 21.5fold higher than that of the wild-type enzyme
F89A
-
site-directed mutagenesis, mutant shows highly increased Km for isopentenyl diphosphate with farnesyl diphosphate and slightly with geranylgeranyl diphosphate compared to the wild-type enzyme
F89A
-
mutation increases (2E,6E)-farnesyl diphosphate and geranylgeranyl diphosphate Km values, indicating that these amino acids are important for substrate binding, but do not determine substrate specificity
L137A
mutant enzyme produces C55-polyprenyl diphosphate, C60-polyprenyl diphosphate and C65-polyprenyl diphosphate in the ratio 55:41:4 in presence of Triton, compared to the wild-type enzyme which produces C55-polyprenyl diphosphate as the major product. In absence of Triton the mutant enzyme produces C70 and C75-polyprenyl diphosphate is the major products
L137A
catalysis results in predominantly the formation of the C70 polymer rather than the C55 polymer
L85A
-
site-directed mutagenesis, mutant shows highly increased Km for isopentenyl diphosphate with farnesyl diphosphate and slightly with geranylgeranyl diphosphate compared to the wild-type enzyme
L85A
-
mutation increases (2E,6E)-farnesyl diphosphate and geranylgeranyl diphosphate Km values, indicating that these amino acids are important for substrate binding, but do not determine substrate specificity
L88A
-
site-directed mutagenesis, mutant shows highly increased Km for isopentenyl diphosphate with farnesyl diphosphate and slightly with geranylgeranyl diphosphate compared to the wild-type enzyme
L88A
-
mutation increases (2E,6E)-farnesyl diphosphate and geranylgeranyl diphosphate Km values, indicating that these amino acids are important for substrate binding, but do not determine substrate specificity
N74A
turnover-number is less than 1% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is equal to that of the wild-type enzyme, the Km-value for isopentenyl diphosphate is 2fold higher than that of the wild-type enzyme
R77A
turnover-number is less than 1% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is 4fold higher than that of the wild-type enzyme, the Km-value for isopentenyl diphosphate is 3.8fold higher than that of the wild-type enzyme
S71A
turnover-number is 4.4% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is 2.5fold higher than that of the wild-type enzyme, the Km-value for isopentenyl diphosphate is 32.4fold higher than that of the wild-type enzyme
W75A
turnover-number is 4.4% of that of the wild-type enzyme, Km-value for farnesyl diphosphate is 8fold higher than that of the wild-type enzyme, the Km-value for isopentenyl diphosphate is 11.2fold higher than that of the wild-type enzyme
C234A
C234A UPPS mutant is crystallized using the hanging drop method, C234A has unchanged kinetic properties compared to wild-type
C234A
site-directed mutagenesis, mutation to prevent intramolecular disulfide bond formed during the long period of crystallization process
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
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
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
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
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 (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
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
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
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
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 (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
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
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
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
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 (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
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 (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
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
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
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
-
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
-
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
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E76Q
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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
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E84Q
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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
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E84Q
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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
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G32R
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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
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G32R
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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
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G32R/R42G
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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
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G32R/R42G
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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
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S74A
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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
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additional information
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gene uppS1 contains a single-point mutation in the ribosome-binding site of the uppS gene. The uppS1 allele is sufficient to confer low-level vancomycin resistance and causes reduced UppS translation. The decreased level of UppS renders Bacillus subtilis slightly more susceptible to many late-acting cell wall antibiotics, including beta-lactams, but significantly more resistant to fosfomycin and D-cycloserine, antibiotics that interfere with the very early steps of cell wall synthesis. The uppS1 allele leads to slightly elevated expression of the sigmaM regulon, possibly helping to compensate for the stress caused by a decrease in UPP levels
additional information
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gene uppS1 contains a single-point mutation in the ribosome-binding site of the uppS gene. The uppS1 allele is sufficient to confer low-level vancomycin resistance and causes reduced UppS translation. The decreased level of UppS renders Bacillus subtilis slightly more susceptible to many late-acting cell wall antibiotics, including beta-lactams, but significantly more resistant to fosfomycin and D-cycloserine, antibiotics that interfere with the very early steps of cell wall synthesis. The uppS1 allele leads to slightly elevated expression of the sigmaM regulon, possibly helping to compensate for the stress caused by a decrease in UPP levels
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additional information
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loop-shortening mutants with deletion of V82 and S83 or S72 also adopt an open conformation with the loop stretched, although they show decreased intrinsic fluorescence with (2E,6E)-farnesyl diphosphate bound, similar to that seen in the wild-type enzyme
additional information
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four uppS deletion mutants of Streptococcus pneumoniae R6 pKO1-4
