1.20.1.1: phosphonate dehydrogenase
This is an abbreviated version!
For detailed information about phosphonate dehydrogenase, go to the full flat file.
Word Map on EC 1.20.1.1
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1.20.1.1
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phosphorus
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stutzeri
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hydride
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baeyer-villiger
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biotechnology
-
bvmos
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phenylacetone
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d-hydroxy
-
synthesis
- 1.20.1.1
- phosphorus
- stutzeri
-
hydride
-
baeyer-villiger
- biotechnology
-
bvmos
- phenylacetone
-
d-hydroxy
- synthesis
Reaction
Synonyms
NAD-dependent phosphite dehydrogenase, NAD:phosphite oxidoreductase, phosphite dehydrogenase, PTDH, PtxD
ECTree
1.20.1.1 phosphonate dehydrogenaseAdvanced search results
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results (Engineering
Engineering on EC 1.20.1.1 - phosphonate dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
R301A
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mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
R301K
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
S295A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation S295A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134F
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mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134F leads to sharp decrease in activity, while kcat value is similar to wild-type
Y139F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
R301A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
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R301K
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
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W134A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
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Y139F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
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R301A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
R301K
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
S295A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation S295A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134F leads to sharp decrease in activity, while kcat value is similar to wild-type
Y139F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
R301A
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
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R301K
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
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W134A
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
-
Y139F
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
-
R301A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
R301K
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
S295A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation S295A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134A
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134F leads to sharp decrease in activity, while kcat value is similar to wild-type
Y139F
-
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
A146S
increases the half-life of thermal inactivation at 45°C from around 1 min to 8 min
A319E
increases the half-life of thermal inactivation at 45°C from around 1 min to 2 min
A319E/T101A
increases the half-life of thermal inactivation at 45°C from around 1 min to 5 min
A325V
thermostability almost identical to that of the wild-type enzyme
C336D
increases solubility and activity, thermostability almost identical to that of the wild-type enzyme
D13E
increases solubility and activity, thermostability almost identical to that of the wild-type enzyme
D13E/M26I/E175A/E332N/C336D
-
mutant obtained by directed evolution, round 4
D13E/M26I/E175A/T181S/A308T/E332N/C336D
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mutant obtained by directed evolution, round 6, strong decrease in KM value for NADP compared to wild-type
D13E/M26I/E175A/T181S/E332N/C336D
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mutant obtained by directed evolution, round 5
D13E/M26I/V71I/E130K/Q132R/Q137R/I150F/E175A/Q215L/R275Q/L276Q/I313L/V315A/A319E/A325V/E332N/C336D
thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity. Mutation E175A leads to relaxation of cofactor specificity
D79A
-
significant differences in its kinetic constants compared to the wild-type enzyme. 2600fold decrease in catalytic efficiency. Pre-steady-state rates are approximately the same as the steady-state rates
E130K
increases the half-life of thermal inactivation at 45°C from around 1 min to 12.5 min
E130Q
increases the half-life of thermal inactivation at 45°C from around 1 min to 7 min
E130R
increases the half-life of thermal inactivation at 45°C from around 1 min to 9 min
E175A
E175A/A176R
E266Q
E332N
increases solubility and activity, thermostability almost identical to that of the wild-type enzyme
F198M
increases the half-life of thermal inactivation at 45°C from around 1 min to 2 min
H292F
H292K
H292N
I150F
I313L
thermostability almost identical to that of the wild-type enzyme
K76A
L276C
increases the half-life of thermal inactivation at 45°C from around 1 min to 12 min
L276H
increases the half-life of thermal inactivation at 45°C from around 1 min to 2 min
L276Q
increases the half-life of thermal inactivation at 45°C from around 1 min to 3.5 min
L276R
increases the half-life of thermal inactivation at 45°C from around 1 min to 8 min
L276S
increases the half-life of thermal inactivation at 45°C from around 1 min to 3 min
M26I
increases solubility and activity, thermostability almost identical to that of the wild-type enzyme
M53A
the KM values for phosphonate and NAD+ are little different from the parent enzyme, while kcat is reduced by a factor of 50
M53N
the KM values for phosphonate and NAD+ are little different from the parent enzyme, while kcat is reduced by a factor of 200
Q132K
increases the half-life of thermal inactivation at 45°C from around 1 min to 3 min
Q132R
Q132R/Q137R/I150F/Q215L/R275Q
-
thermostable mutant, half-life at 45°C 161 min compared to 1.4 min of wild-type
Q137H
increases the half-life of thermal inactivation at 45°C from around 1 min to 4.5 min
Q137R
Q137R/I150F/Q215L/R275Q
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thermostable mutant, half-life at 45°C 200 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/A319E
-
thermostable mutant, half-life at 45°C 567 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/D162N/V315A
-
thermostable mutant, half-life at 45°C 614 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q
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thermostable mutant, half-life at 45°C 437 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A
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thermostable mutant, half-life at 45°C 1421 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/A325V
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thermostable mutant, half-life at 45°C 2315 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/E130K
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thermostable mutant, half-life at 45°C 1515 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/I313L
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thermostable mutant, half-life at 45°C 1765 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R
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thermostable mutant, half-life at 45°C 2350 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R/V71I/E130K/I313L/A325V
-
thermostable mutant, half-life at 45°C 8440 min compared to 1.4 min of wild-type
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/Q132R/V71I/E130K/I313L/A325V/A176R
-
highly stable and active mutant engineered for regeneration of NADPH and enzyme membrane reactors
Q137R/I150F/Q215L/R275Q/L276Q/A319E/V315A/V71I
-
thermostable mutant, half-life at 45°C 2000 min compared to 1.4 min of wild-type
Q215L
Q215M
increases the half-life of thermal inactivation at 45°C from around 1 min to 2.5 min
R237K
R275L
increases the half-life of thermal inactivation at 45°C from around 1 min to 9 min
R275Q
R301A
R301K
S295A
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation S295A leads to sharp decrease in activity, while kcat value is similar to wild-type
T101A
increases the half-life of thermal inactivation at 45°C from around 1 min to 4.5 min
V315A
thermostability almost identical to that of the wild-type enzyme
V71Ia
thermostability almost identical to that of the wild-type enzyme
W134A
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134A leads to sharp decrease in activity, while kcat value is similar to wild-type
W134F
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation W134F leads to sharp decrease in activity, while kcat value is similar to wild-type
Y139F
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation Y139F leads to sharp decrease in activity, while kcat value is similar to wild-type
E266Q
-
significant increase in Km for both substrates, increase in turnover
-
E175A/A176R
-
double mutant, 3.6-fold higher efficiency with NAD+, 1000-fold higher efficiency with NADP+, 3-fold favor for NADP+ over NAD+ as cofactor
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M53A
-
the KM values for phosphonate and NAD+ are little different from the parent enzyme, while kcat is reduced by a factor of 50
-
M53N
-
the KM values for phosphonate and NAD+ are little different from the parent enzyme, while kcat is reduced by a factor of 200
-
R301A
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the mutant shows about 100fold loss in kcat and a 500fold increased Km value for phosphonate. The Ki value of sulfite with the mutant is 400fold increased compared to the wild type enzyme
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R301K
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the mutant exhibits a slightly higher kcat than the wild type enzyme and a 20fold increased Km value for phosphonate
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D79A
-
significant differences in its kinetic constants compared to the wild-type enzyme. 2600fold decrease in catalytic efficiency. Pre-steady-state rates are approximately the same as the steady-state rates
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E266Q
-
higher activity, steady-state and pre-steady-state rates are comparable
-
K76A
-
pre-steady-state rates are approximately the same as the steady-state rates
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R237K
-
low activity, absence of a significant burst in the pre-steady-state
-
additional information
E175A
increases solubility and activity, thermostability almost identical to that of the wild-type enzyme
E175A/A176R
-
double mutant, 3.6-fold higher efficiency with NAD+, 1000-fold higher efficiency with NADP+, 3-fold favor for NADP+ over NAD+ as cofactor
E175A/A176R
-
mutant utilizes both NAD+ and NADP+, kinetic isotope effects study, hydride transfer step is partially rate determining
E266Q
-
significant increase in Km for both substrates, increase in turnover
E266Q
-
higher activity, steady-state and pre-steady-state rates are comparable
I150F
-
thermostable mutant, half-life at 45°C 7.0 min compared to 1.4 min of wild-type
I150F
increases the half-life of thermal inactivation at 45°C from around 1 min to 7 min
K76A
-
pre-steady-state rates are approximately the same as the steady-state rates
Q132R
-
thermostable mutant, half-life at 45°C 2.3 min compared to 1.4 min of wild-type
Q132R
increases the half-life of thermal inactivation at 45°C from around 1 min to 2 min
Q137R
-
thermostable mutant, half-life at 45°C 3.8 min compared to 1.4 min of wild-type
Q137R
increases the half-life of thermal inactivation at 45°C from around 1 min to 4 min
Q215L
-
thermostable mutant, half-life at 45°C 8.7 min compared to 1.4 min of wild-type
Q215L
increases the half-life of thermal inactivation at 45°C from around 1 min to 9 min
R237K
-
low activity, absence of a significant burst in the pre-steady-state
R275Q
-
thermostable mutant, half-life at 45°C 4.6 min compared to 1.4 min of wild-type
R275Q
increases the half-life of thermal inactivation at 45°C from around 1 min to 4.5 min
R301A
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301A leads to sharp decrease in activity, while kcat value is similar to wild-type
R301A
the mutant shows about 100fold loss in kcat and a 500fold increased Km value for phosphonate. The Ki value of sulfite with the mutant is 400fold increased compared to the wild type enzyme
R301K
mutant based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+. Mutation R301K leads to sharp decrease in activity, while kcat value is similar to wild-type
R301K
the mutant exhibits a slightly higher kcat than the wild type enzyme and a 20fold increased Km value for phosphonate
additional information
-
mutant 17x-PTDH is based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+
additional information
-
mutant 17x-PTDH is based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+
-
additional information
-
mutant 17x-PTDH is based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+
additional information
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
mutant 17x-PTDH is based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+
-
additional information
-
mutant 17x-PTDH is based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+
additional information
12 x PTDH mutant, saturation mutagenesis performed separately on each of the following residues in the parent PTDH template: V71, E130, Q132, Q137, I150, Q215, R275, L276, I313, V315, A319, and A325. The most thermostabilizing mutation discovered for each particular site is incorporated into the 12 x PTDH mutant, performed for K132, H137, L275, and C276, forming an optimized thermally stable phosphite dehydrogenase termed Opt12. Addition of A146S to Opt12 leads to the Opt13 variant, and the further addition of F198M leads to Opt14
additional information
-
thermostable mutant 12X-PTDH with higher solubility than the wild-type. Thermostable mutant with dual cofactor specificity NADP-12X NAD shows pre-steady-state behavior very similar to that observed with 12X-PTDH and the wild-type enzyme. Pre-steady-state traces of thermostable mutant with dual cofactor specificity NADP-12X NADP shows curvature with NADP, particularly with protiated phosphite
additional information
mutant 17x-PTDH is based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+
additional information
-
mutant 17x-PTDH is based on a thermostable mutant TS-PTDH which contains 12 mutations that result in considerably increased thermostability with minimal change in activity, and four additional mutations that increase its activity, plus mutation E175A that allows this mutant to use both NAD+ and NADP+
additional information
-
thermostable mutant 12X-PTDH with higher solubility than the wild-type. Thermostable mutant with dual cofactor specificity NADP-12X NAD shows pre-steady-state behavior very similar to that observed with 12X-PTDH and the wild-type enzyme. Pre-steady-state traces of thermostable mutant with dual cofactor specificity NADP-12X NADP shows curvature with NADP, particularly with protiated phosphite
-
