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Literature summary for 2.5.1.31 extracted from

  • Ko, T.P.; Chen, Y.K.; Robinson, H.; Tsai, P.C.; Gao, Y.G.; Chen, A.P.C.; Wang, A.H.J.; Liang, P.H.
    Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis (2001), J. Biol. Chem., 276, 47474-47482.
    View publication on PubMed
Search for more literature for 2.5.1.31

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop method Escherichia coli

Protein Variants

Protein Variants Comment Organism
A143V the C30 intermediate is formed to a greater extent and is longer lived in the process catalyzed by the A69L mutant Escherichia coli
A69L the small side chain of Ala-69 is required for rapid elongation to the C55 product Escherichia coli
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 Escherichia coli
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 Escherichia coli
E81A increases in the IPP Km values Escherichia coli
H103A the product distributions formed by the use of the I62A, V105A, and H103A mutants are similar to those observed for wild-type UPPs Escherichia coli
I62A the product distributions formed by the use of the I62A, V105A, and H103A mutants are similar to those observed for wild-type UPPs Escherichia coli
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 Escherichia coli
L137A catalysis results in predominantly the formation of the C70 polymer rather than the C55 polymer Escherichia coli
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 Escherichia coli
N74A decrease in kcat values Escherichia coli
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 Escherichia coli
R77A decrease in kcat values Escherichia coli
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 Escherichia coli
S71A decrease in kcat values Escherichia coli
S71A increases in the IPP Km values Escherichia coli
V105A the product distributions formed by the use of the I62A, V105A, and H103A mutants are similar to those observed for wild-type UPPs Escherichia coli
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 Escherichia coli
W75A shows 8fold increase of the FPP Km value Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0004
-
 farnesyl diphosphate wild-type enzyme, pH 7.5, 25°C Escherichia coli
0.0004
-
 farnesyl diphosphate mutant enzyme E73A, N74A and E81A, pH 7.5, 25°C Escherichia coli
0.0004
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, wild type Escherichia coli
0.0004
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, E73A mutant Escherichia coli
0.0004
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, E81A mutant Escherichia coli
0.0004
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, N74A mutant Escherichia coli
0.001
-
 farnesyl diphosphate mutant enzyme S71A, pH 7.5, 25°C Escherichia coli
0.001
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, S71A mutant Escherichia coli
0.0016
-
 farnesyl diphosphate mutant enzyme R77A, pH 7.5, 25°C Escherichia coli
0.0016
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, R77A mutant Escherichia coli
0.0032
-
 farnesyl diphosphate mutant enzyme W75A, pH 7.5, 25°C Escherichia coli
0.0032
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, W75A mutant Escherichia coli
0.0041
-
 isopentenyl diphosphate pH 7.5, 25°C Escherichia coli
0.0041
-
 isopentenyl diphosphate pH 7.5, 25°C, wild type Escherichia coli
0.008
-
 isopentenyl diphosphate mutant enzyme N74A, pH 7.5, 25°C Escherichia coli
0.008
-
 isopentenyl diphosphate pH 7.5, 25°C, N74A mutant Escherichia coli
0.0157
-
 isopentenyl diphosphate mutant enzyme R77A, pH 7.5, 25°C Escherichia coli
0.0157
-
 isopentenyl diphosphate pH 7.5, 25°C, R77A mutant Escherichia coli
0.0162
-
 isopentenyl diphosphate mutant enzyme E73A, pH 7.5, 25°C Escherichia coli
0.0162
-
 isopentenyl diphosphate pH 7.5, 25°C, E73A mutant Escherichia coli
0.046
-
 isopentenyl diphosphate mutant enzyme W75A, pH 7.5, 25°C Escherichia coli
0.046
-
 isopentenyl diphosphate pH 7.5, 25°C, W75A mutant Escherichia coli
0.088
-
 isopentenyl diphosphate mutant enzyme E81A, pH 7.5, 25°C Escherichia coli
0.088
-
 isopentenyl diphosphate pH 7.5, 25°C, E81A mutant Escherichia coli
0.133
-
 isopentenyl diphosphate mutant enzyme S71A, pH 7.5, 25°C Escherichia coli
0.133
-
 isopentenyl diphosphate pH 7.5, 25°C, S71A mutant Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli P60472
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate
-
 Escherichia coli 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
-
 ?
isopentenyl diphosphate + farnesyl diphosphate
-
 Escherichia coli C55-polyprenyl diphosphate + C50-polyprenyl diphosphate + diphosphate the major product of the wild-type enzyme, and mutant enzymes H103A, V103A, V105A and I62A in presence of Triton is C55-polyprenyl diphosphate. Mutant enzyme L137A produces C55-polyprenyl diphosphate, C60-polyprenyl diphosphate and C65-polyprenyl diphosphate in the ration 55:41:4 ?

Synonyms

Synonyms Comment Organism
undecaprenyl-pyrophosphate synthase
-
 Escherichia coli
UPPs
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Escherichia coli
0.00014
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, R77A mutant Escherichia coli
0.022
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, N74A mutant Escherichia coli
0.11
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, S71A mutant Escherichia coli
0.3
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, E73A mutant Escherichia coli
0.4
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, E81A mutant Escherichia coli
1.1
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, W75A mutant Escherichia coli
2.5
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, wild type Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0875
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, R77A mutant Escherichia coli
55
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, N74A mutant Escherichia coli
110
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, S71A mutant Escherichia coli
344
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, W75A mutant Escherichia coli
750
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, E73A mutant Escherichia coli
1000
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, E81A mutant Escherichia coli
6250
-
 (2E,6E)-farnesyl diphosphate pH 7.5, 25°C, wild type Escherichia coli