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1-butanol + phenazine ethosulfate
butyraldehyde + reduced phenazine ethosulfate
1-butanol + phenazine methosulfate
butyraldehyde + reduced phenazine methosulfate
1-hexanol + phenazine ethosulfate
hexaldehyde + reduced phenazine ethosulfate
1-hexanol + phenazine methosulfate
hexaldehyde + reduced phenazine methosulfate
1-propanol + phenazine ethosulfate
propionaldehyde + reduced phenazine ethosulfate
1-propanol + phenazine methosulfate
propionaldehyde + reduced phenazine methosulfate
2-propanol + phenazine ethosulfate
?
2-propanol + phenazine methosulfate
?
acetaldehyde + reduced phenazine ethosulfate
ethanol + phenazine ethosulfate
-
less than 50% activity compared to methanol
-
-
?
acetaldehyde + reduced phenazine methosulfate
ethanol + phenazine methosulfate
ethanol + phenazine ethosulfate
acetaldehyde + reduced phenazine ethosulfate
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
formaldehyde + phenazine methosulfate + ?
formate + reduced phenazine methosulfate + ?
formaldehyde + reduced phenazine ethosulfate
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine methosulfate
methanol + phenazine methosulfate
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
methanol + 2 oxidized cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
methanol + oxidized cytochrome c XoxG
formaldehyde + reduced cytochrome c XoxG
-
-
-
-
?
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
methanol + phenazine methosulfate
formaldehyde + reduced phenazine ethosulfate
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
methanol + Wurster's Blue
formaldehyde + ?
propionaldehyde + reduced phenazine methosulfate
1-propanol + phenazine methosulfate
additional information
?
-
1-butanol + phenazine ethosulfate
butyraldehyde + reduced phenazine ethosulfate
-
78.3% activity compared to methanol
-
-
r
1-butanol + phenazine ethosulfate
butyraldehyde + reduced phenazine ethosulfate
-
78.3% activity compared to methanol
-
-
r
1-butanol + phenazine ethosulfate
butyraldehyde + reduced phenazine ethosulfate
-
100% activity compared to methanol
-
-
?
1-butanol + phenazine ethosulfate
butyraldehyde + reduced phenazine ethosulfate
-
100% activity compared to methanol
-
-
?
1-butanol + phenazine methosulfate
butyraldehyde + reduced phenazine methosulfate
-
more than 95% activity compared to methanol
-
-
r
1-butanol + phenazine methosulfate
butyraldehyde + reduced phenazine methosulfate
-
more than 95% activity compared to methanol
-
-
r
1-hexanol + phenazine ethosulfate
hexaldehyde + reduced phenazine ethosulfate
-
100% activity compared to methanol
-
-
?
1-hexanol + phenazine ethosulfate
hexaldehyde + reduced phenazine ethosulfate
-
100% activity compared to methanol
-
-
?
1-hexanol + phenazine methosulfate
hexaldehyde + reduced phenazine methosulfate
-
more than 95% activity compared to methanol
-
-
r
1-hexanol + phenazine methosulfate
hexaldehyde + reduced phenazine methosulfate
-
more than 95% activity compared to methanol
-
-
r
1-propanol + phenazine ethosulfate
propionaldehyde + reduced phenazine ethosulfate
-
85.3% activity compared to methanol
-
-
r
1-propanol + phenazine ethosulfate
propionaldehyde + reduced phenazine ethosulfate
-
85.3% activity compared to methanol
-
-
r
1-propanol + phenazine ethosulfate
propionaldehyde + reduced phenazine ethosulfate
-
100% activity compared to methanol
-
-
?
1-propanol + phenazine methosulfate
propionaldehyde + reduced phenazine methosulfate
-
more than 95% activity compared to methanol
-
-
r
1-propanol + phenazine methosulfate
propionaldehyde + reduced phenazine methosulfate
-
more than 95% activity compared to methanol
-
-
r
1-propanol + phenazine methosulfate
propionaldehyde + reduced phenazine methosulfate
-
more than 95% activity compared to methanol
-
-
r
2-propanol + phenazine ethosulfate
?
-
0.775% activity compared to methanol
-
-
r
2-propanol + phenazine ethosulfate
?
-
0.775% activity compared to methanol
-
-
r
2-propanol + phenazine methosulfate
?
-
40% activity compared to methanol
-
-
r
2-propanol + phenazine methosulfate
?
-
subtype XoxF4-1 shows 20% activity compared to methanol, subtype XoxF4-2 shows 5% activity compared to methanol
-
-
r
acetaldehyde + reduced phenazine methosulfate
ethanol + phenazine methosulfate
-
60% activity compared to methanol
-
-
r
acetaldehyde + reduced phenazine methosulfate
ethanol + phenazine methosulfate
-
subtype XoxF4-1 shows 50% activity compared to methanol, subtype XoxF4-2 shows 15% activity compared to methanol
-
-
r
acetaldehyde + reduced phenazine methosulfate
ethanol + phenazine methosulfate
-
subtype XoxF4-1 shows 50% activity compared to methanol, subtype XoxF4-2 shows 15% activity compared to methanol
-
-
r
ethanol + phenazine ethosulfate
acetaldehyde + reduced phenazine ethosulfate
-
93% activity compared to methanol
-
-
r
ethanol + phenazine ethosulfate
acetaldehyde + reduced phenazine ethosulfate
-
93% activity compared to methanol
-
-
r
ethanol + phenazine ethosulfate
acetaldehyde + reduced phenazine ethosulfate
-
100% activity compared to methanol
-
-
?
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
-
more than 95% activity compared to methanol
-
-
r
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
highest activity
-
-
r
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
-
best substrate for ExaF
-
-
?
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
-
more than 95% activity compared to methanol
-
-
r
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
-
more than 95% activity compared to methanol
-
-
r
formaldehyde + phenazine methosulfate + ?
formate + reduced phenazine methosulfate + ?
-
-
-
?
formaldehyde + phenazine methosulfate + ?
formate + reduced phenazine methosulfate + ?
-
-
-
?
formaldehyde + reduced phenazine ethosulfate
methanol + phenazine ethosulfate
-
91.5% activity compared to methanol
-
-
r
formaldehyde + reduced phenazine ethosulfate
methanol + phenazine ethosulfate
-
100% activity compared to methanol
-
-
r
formaldehyde + reduced phenazine methosulfate
methanol + phenazine methosulfate
-
more than 95% activity compared to methanol
-
-
r
formaldehyde + reduced phenazine methosulfate
methanol + phenazine methosulfate
the enzyme is 100times more efficient at oxidizing formaldehyde than methanol
-
-
r
formaldehyde + reduced phenazine methosulfate
methanol + phenazine methosulfate
-
more than 95% activity compared to methanol
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
electrochemic reaction, use of a Au/MU electrode for the electrontransfer process. The attenuation coefficient of DCPIP is known to be very sensitive to changes in pH, reactions with DCPIP are monitored at 600 nm
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
electrochemical redox reaction
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
electrochemical redox reaction
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
electrochemic reaction, use of a Au/MU electrode for the electrontransfer process. The attenuation coefficient of DCPIP is known to be very sensitive to changes in pH, reactions with DCPIP are monitored at 600 nm
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
r
methanol + 2 oxidized cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
?
methanol + 2 oxidized cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
c-type cytochrome XoxG
-
-
?
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
-
100% activity
-
-
r
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
-
100% activity
-
-
r
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
-
-
-
-
?
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
-
100% activity
-
-
r
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
-
-
-
-
?
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
-
100% activity
-
-
r
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
-
-
-
-
?
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
-
-
-
?
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine ethosulfate
-
methanol is the preferred substrate
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine ethosulfate
-
methanol is the preferred substrate
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine ethosulfate
-
methanol is the preferred substrate
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine ethosulfate
-
methanol is the preferred substrate
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
methanol is the preferred substrate
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
methanol is the preferred substrate
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
100% activity
-
-
r
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
phenazine methosulfate or phenazine ethosulfate and DCPIP coupled assay is the method of choice for methynol dehydrogenasae kinetic analysis and can yield reproducible results when the components are handled correctly
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
100% activity
-
-
r
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
phenazine methosulfate or phenazine ethosulfate and DCPIP coupled assay is the method of choice for methynol dehydrogenasae kinetic analysis and can yield reproducible results when the components are handled correctly
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
100% activity
-
-
r
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
methanol is the preferred substrate
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
r
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
best substrate for XoxF1
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
methanol is the preferred substrate
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
phenazine methosulfate or phenazine ethosulfate and DCPIP coupled assay is the method of choice for methynol dehydrogenasae kinetic analysis and can yield reproducible results when the components are handled correctly
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
100% activity
-
-
r
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
methanol is the preferred substrate
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
100% activity
-
-
r
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
methanol is the preferred substrate
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
methanol is the preferred substrate
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
methanol is the preferred substrate
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
methanol is the preferred substrate
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
methanol is the preferred substrate
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
methanol is the preferred substrate
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
methanol is the preferred substrate
-
-
?
methanol + Wurster's Blue
formaldehyde + ?
-
the one-electron acceptor and dye Wurster's Blue presents an easy method for routine methanol dehydrogenase assays, for example, identifying methanol dehydrogenase containing fractions during enzyme purification. Due to its low stability at alkaline pH, phenazine ethosulfate-2,6-dichlorophenolindophenol is preferable to Wurster's Blue as electron acceptor/dye for determining the kinetic parameters
-
-
?
methanol + Wurster's Blue
formaldehyde + ?
-
the one-electron acceptor and dye Wurster's Blue presents an easy method for routine methanol dehydrogenase assays, for example, identifying methanol dehydrogenase containing fractions during enzyme purification. Due to its low stability at alkaline pH, phenazine ethosulfate-2,6-dichlorophenolindophenol is preferable to Wurster's Blue as electron acceptor/dye for determining the kinetic parameters
-
-
?
methanol + Wurster's Blue
formaldehyde + ?
the one-electron acceptor and dye Wurster's Blue presents an easy method for routine methanol dehydrogenase assays, for example, identifying methanol dehydrogenase containing fractions during enzyme purification. Due to its low stability at alkaline pH, phenazine ethosulfate-2,6-dichlorophenolindophenol is preferable to Wurster's Blue as electron acceptor/dye for determining the kinetic parameters
-
-
?
propionaldehyde + reduced phenazine methosulfate
1-propanol + phenazine methosulfate
-
60% activity compared to methanol
-
-
r
propionaldehyde + reduced phenazine methosulfate
1-propanol + phenazine methosulfate
-
subtype XoxF4-1 shows 50% activity compared to methanol, subtype XoxF4-2 shows 15% activity compared to methanol
-
-
r
propionaldehyde + reduced phenazine methosulfate
1-propanol + phenazine methosulfate
-
subtype XoxF4-1 shows 50% activity compared to methanol, subtype XoxF4-2 shows 15% activity compared to methanol
-
-
r
additional information
?
-
-
no activity with 2-propanol and formate
-
-
-
additional information
?
-
-
no activity with 2-propanol and formate
-
-
-
additional information
?
-
for assay of chromatography fractions during purifications, activity can be determined by reduction of 2,6-dichlorophenolindolphenol (DCPIP) using phenazine ethosulfate (PES) as an electron acceptor. Development of ddifferent assay methods, detailed overview
-
-
-
additional information
?
-
-
MDH activity is also spectrophotometrically monitored via the reduction of 2,6-dichlorophenolindophenol (DCPIP) by the MDH with either phenazine ethosulfate or phenazine methosulfate as mediator. XoxG exhibits an unusually low reduction potential. The reduction potential of XoxG may be specifically optimized for transfer of electrons from PQQ, bound to lighter LnIIIs, to the cytochrome
-
-
-
additional information
?
-
MDH activity is also spectrophotometrically monitored via the reduction of 2,6-dichlorophenolindophenol (DCPIP) by the MDH with either phenazine ethosulfate or phenazine methosulfate as mediator. XoxG exhibits an unusually low reduction potential. The reduction potential of XoxG may be specifically optimized for transfer of electrons from PQQ, bound to lighter LnIIIs, to the cytochrome
-
-
-
additional information
?
-
MDH activity is also spectrophotometrically monitored via the reduction of 2,6-dichlorophenolindophenol (DCPIP) by the MDH with either phenazine ethosulfate or phenazine methosulfate as mediator. XoxG exhibits an unusually low reduction potential. The reduction potential of XoxG may be specifically optimized for transfer of electrons from PQQ, bound to lighter LnIIIs, to the cytochrome
-
-
-
additional information
?
-
for assay of chromatography fractions during purifications, activity can be determined by reduction of 2,6-dichlorophenolindolphenol (DCPIP) using phenazine ethosulfate (PES) as an electron acceptor. Development of ddifferent assay methods, detailed overview
-
-
-
additional information
?
-
MDH activity is also spectrophotometrically monitored via the reduction of 2,6-dichlorophenolindophenol (DCPIP) by the MDH with either phenazine ethosulfate or phenazine methosulfate as mediator. XoxG exhibits an unusually low reduction potential. The reduction potential of XoxG may be specifically optimized for transfer of electrons from PQQ, bound to lighter LnIIIs, to the cytochrome
-
-
-
additional information
?
-
for assay of chromatography fractions during purifications, activity can be determined by reduction of 2,6-dichlorophenolindolphenol (DCPIP) using phenazine ethosulfate (PES) as an electron acceptor. Development of ddifferent assay methods, detailed overview
-
-
-
additional information
?
-
MDH activity is also spectrophotometrically monitored via the reduction of 2,6-dichlorophenolindophenol (DCPIP) by the MDH with either phenazine ethosulfate or phenazine methosulfate as mediator. XoxG exhibits an unusually low reduction potential. The reduction potential of XoxG may be specifically optimized for transfer of electrons from PQQ, bound to lighter LnIIIs, to the cytochrome
-
-
-
additional information
?
-
for assay of chromatography fractions during purifications, activity can be determined by reduction of 2,6-dichlorophenolindolphenol (DCPIP) using phenazine ethosulfate (PES) as an electron acceptor. Development of ddifferent assay methods, detailed overview
-
-
-
additional information
?
-
MDH activity is also spectrophotometrically monitored via the reduction of 2,6-dichlorophenolindophenol (DCPIP) by the MDH with either phenazine ethosulfate or phenazine methosulfate as mediator. XoxG exhibits an unusually low reduction potential. The reduction potential of XoxG may be specifically optimized for transfer of electrons from PQQ, bound to lighter LnIIIs, to the cytochrome
-
-
-
additional information
?
-
for assay of chromatography fractions during purifications, activity can be determined by reduction of 2,6-dichlorophenolindolphenol (DCPIP) using phenazine ethosulfate (PES) as an electron acceptor. Development of ddifferent assay methods, detailed overview
-
-
-
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Ca2+
-
the purified enzyme contains 0.39 atoms of Ca2+ per dimer
Fe2+
in heme and bound to XoxG
Ce3+
-
highest activity with 0.03 mM Ce3+. The enzyme contains 0.58 cerium atoms per subunit
Ce3+
-
lanthanide-dependent enzyme
Ce3+
the strain Ce-3 is able to grow in a media containing methanol as a sole carbon source and light lanthanides (i.e., La3+, Ce3+, Pr3+, and Nd3+), whereas the strain does not show any growth with Ca2+ or the heavy lanthanide, Sm3+
Ce3+
-
the enzyme contains a cerium ion in the active site
Ce3+
-
lanthanide-dependent enzyme
Ce3+
-
remarkable activation
Ce3+
-
lanthanide-dependent enzyme
Ce3+
a lanthanide is required
Ce3+
-
lanthanide-dependent enzyme
Dy3+
-
lanthanide-dependent enzyme
Dy3+
lanthanide-dependent enzyme. The enzyme binds La3+ with higher affinity than Ca2+. The binding of heavier lanthanides is preferred over the binding of La3+, with Gd3+ showing the highest affinity of all Ln3+ ions that are tested (La3+, Sm3+, Gd3+, Dy3+, and Lu3+)
Eu3+
-
the addition of increasing amounts of europium(III) to 200 nM purified partial-apo enzyme leads to a gradual increase in activity until saturation around 0.005 to 0.02 mM added metal is observed
Eu3+
-
lanthanide-dependent enzyme
Eu3+
-
the enzyme is dependent on the lanthanide europium
Gd3+
-
activates
Gd3+
lanthanide-dependent enzyme. The enzyme binds La3+ with higher affinity than Ca2+. The binding of heavier lanthanides is preferred over the binding of La3+, with Gd3+ showing the highest affinity of all Ln3+ ions that are tested (La3+, Sm3+, Gd3+, Dy3+, and Lu3+)
La3+
-
second highest activity with 0.03 mM La3+
La3+
-
lanthanide-dependent enzyme
La3+
the strain Ce-3 is able to grow in a media containing methanol as a sole carbon source and light lanthanides (i.e., La3+, Ce3+, Pr3+, and Nd3+), whereas the strain does not show any growth with Ca2+ or the heavy lanthanide, Sm3+
La3+
-
lanthanide-dependent enzyme
La3+
-
between 0 and 0.005 mM La3+ a sharp increase in enzyme activity is observed
La3+
-
lanthanide-dependent enzyme
La3+
-
required, 0.03 mM used in assay conditions
La3+
lanthanides are an essential cofactor for XoxF-type methanol dehydrogenases
La3+
-
570% activity at 0.03 mM
La3+
-
dependent on. Low activity of the enzyme is detected at 0.003 mM La3+, gradually increasing with the concentration of La3+ (0.003-0.06 mM)
La3+
-
lanthanide-dependent enzyme
La3+
-
activates, 0.002 mM used in assay conditions
La3+
-
dependent on. XoxF1 contains La3+ in 1:1 molar ratio of metal to protomer
La3+
-
the enzyme is activated by La3+. The purified enzyme contains 0.91 atoms of La3+ atoms per dimer
La3+
the enzyme preferentially binds La3+ over Ca2+ in the active site. 0.1 mM used in assay conditions. The enzyme contains 1.3 mol of La3+ per mol of protomer
La3+
a lanthanide is required
La3+
-
lanthanide-dependent enzyme
La3+
lanthanide-dependent enzyme
La3+
lanthanide-dependent enzyme. Although La3+ and Nd3+ have similar distributions in nature, XoxF can chose La3+ preferentially, likely because of its higher Lewis acidity, which is important for the catalytic activity of the enzyme
La3+
-
lanthanide-dependent enzyme
La3+
-
required for activity
La3+
-
contains a La3+ ion in the active site
La3+
lanthanide-dependent enzyme. The enzyme binds La3+ with higher affinity than Ca2+. The binding of heavier lanthanides is preferred over the binding of La3+, with Gd3+ showing the highest affinity of all Ln3+ ions that are tested (La3+, Sm3+, Gd3+, Dy3+, and Lu3+)
La3+
lanthanide-dependent enzyme
La3+
-
lanthanide-dependent enzyme
La3+
-
lanthanide-dependent enzyme
La3+
-
lanthanide-dependent enzyme
Lu3+
-
lanthanide-dependent enzyme
Lu3+
lanthanide-dependent enzyme. The enzyme binds La3+ with higher affinity than Ca2+. The binding of heavier lanthanides is preferred over the binding of La3+, with Gd3+ showing the highest affinity of all Ln3+ ions that are tested (La3+, Sm3+, Gd3+, Dy3+, and Lu3+)
Nd3+
-
activates at 0.03 mM
Nd3+
-
lanthanide-dependent enzyme
Nd3+
the strain Ce-3 is able to grow in a media containing methanol as a sole carbon source and light lanthanides (i.e., La3+, Ce3+, Pr3+, and Nd3+), whereas the strain does not show any growth with Ca2+ or the heavy lanthanide, Sm3+
Nd3+
-
lanthanide-dependent enzyme
Nd3+
-
between 0 and 0.005 mM La3+ a sharp increase in enzyme activity is observed
Nd3+
-
lanthanide-dependent enzyme
Nd3+
-
lanthanide-dependent enzyme
Nd3+
a lanthanide is required
Nd3+
-
lanthanide-dependent enzyme
Nd3+
lanthanide-dependent enzyme
Nd3+
lanthanide-dependent enzyme. Although La3+ and Nd3+ have similar distributions in nature, XoxF can chose La3+ preferentially, likely because of its higher Lewis acidity, which is important for the catalytic activity of the enzyme
Nd3+
lanthanide-dependent enzyme
Nd3+
-
lanthanide-dependent enzyme
Nd3+
-
lanthanide-dependent enzyme
Nd3+
-
lanthanide-dependent enzyme
Pr3+
-
activates at 0.03 mM
Pr3+
the strain Ce-3 is able to grow in a media containing methanol as a sole carbon source and light lanthanides (i.e., La3+, Ce3+, Pr3+, and Nd3+), whereas the strain does not show any growth with Ca2+ or the heavy lanthanide, Sm3+
Pr3+
-
between 0 and 0.005 mM La3+ a sharp increase in enzyme activity is observed
Pr3+
-
lanthanide-dependent enzyme
Sm3+
-
slight activation
Sm3+
lanthanide-dependent enzyme. The enzyme binds La3+ with higher affinity than Ca2+. The binding of heavier lanthanides is preferred over the binding of La3+, with Gd3+ showing the highest affinity of all Ln3+ ions that are tested (La3+, Sm3+, Gd3+, Dy3+, and Lu3+)
additional information
-
the enzyme does not require ammonium ions for activation
additional information
-
the enzyme is completely independent of ammonium
additional information
-
not activated by Ca2+
additional information
-
the enzyme has a requirement for ammonia
additional information
-
the enzyme preferentially uses lanthanides over calcium even when lanthanides are present at a 10fold-lower concentration
additional information
lanthanides, especially the lighter and most abundant members (La, Ce, Pr, Nd, Sm, and Eu) of the lanthanide (Ln) series, are essential for catalysis in the most broadly distributed class of pyrroloquinoline quinone (PQQ)-dependent methanol dehydrogenases (MDHs). The number of distinct lanthanides supporting catalysis in vitro and/or in vivo differs from enzyme to enzyme: e.g. La-Nd, La-Sm/Eu, or La-Gd, according to the XoxF clade, in which an enzyme is found. Strain AM1 XoxF1 can be activated in vivo with La, Ce, Pr, and Nd, and poorly or not at all with Sm. The lanthanides are incorporated when they are added individually to the growth media, XoxF expressed in the presence of La, either from endogenous levels or recombinantly in a methylotroph, show roughly stoichiometric La incorporation, Nd incorporation is more variable. By contrast, plasmid-based expression of XoxF in the presence of Nd leads to substoichiometric Nd insertion into XoxF
additional information
-
XoxF has maximal activity in the standard artificial dye-linked assay when metallated with Pr and Nd. Activity is about 30% lower with La and falls off quickly beyond Nd. This biphasic behavior is attributed to competition between the Lewis acidity of the LnIII ion, increasing across the series and therefore enhancing reactivity of the pyrroloquinoline quinone (PQQ) cofactor, with other, opposing factors
additional information
XoxF has maximal activity in the standard artificial dye-linked assay when metallated with Pr and Nd. Activity is about 30% lower with La and falls off quickly beyond Nd. This biphasic behavior is attributed to competition between the Lewis acidity of the LnIII ion, increasing across the series and therefore enhancing reactivity of the pyrroloquinoline quinone (PQQ) cofactor, with other, opposing factors
additional information
-
subtype XoxF4-1 can use lighter lanthanides up to the atomic number of 64 (La3+ through Gd3+) while subtype XoxF4-2 can only use lanthanides up to the atomic number of 62 (La3+ through Sm3+)
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0.0025 - 0.0076
cytochrome cGJ
-
0.007 - 0.815
formaldehyde
0.0025 - 0.0076
oxidized cytochrome cL
-
additional information
additional information
-
0.006
1-butanol
-
at pH 7.0 and 40-45°C
0.096
1-butanol
-
at pH 9.0 and 26°C
0.188
1-butanol
-
subtype XoxF4-1, at pH 9.0 and 26°C
0.47
1-butanol
-
subtype XoxF4-2, at pH 9.0 and 26°C
0.002
1-Hexanol
-
at pH 7.0 and 40-45°C
0.037
1-Hexanol
-
subtype XoxF4-1, at pH 9.0 and 26°C
0.04
1-Hexanol
-
at pH 9.0 and 26°C
0.357
1-Hexanol
-
subtype XoxF4-2, at pH 9.0 and 26°C
0.007
1-propanol
-
at pH 7.0 and 40-45°C
0.061
1-propanol
-
subtype XoxF4-1, at pH 9.0 and 26°C
0.133
1-propanol
-
at pH 9.0 and 26°C
0.873
1-propanol
-
subtype XoxF4-2, at pH 9.0 and 26°C
0.2
acetaldehyde
-
Km above 0.2 mM, at pH 7.0 and 40-45°C
0.285
acetaldehyde
at pH 9.0 and 30°C
0.0025
cytochrome cGJ
pH 7.0, 22°C, La-XoxF
-
0.0076
cytochrome cGJ
pH 7.0, 22°C, Nd-XoxF
-
0.0009
ethanol
at pH 9.0 and 30°C
0.003
ethanol
-
at pH 7.0 and 40-45°C
0.014
ethanol
-
XoxF1, in the absence of lanthanides, pH and temperature not specified in the publication
0.059
ethanol
-
subtype XoxF4-1, at pH 9.0 and 26°C
0.067
ethanol
-
XoxF1, in the presence of La3+, pH and temperature not specified in the publication
0.085
ethanol
-
at pH 9.0 and 26°C
0.515
ethanol
-
subtype XoxF4-2, at pH 9.0 and 26°C
0.007
formaldehyde
-
at pH 7.0 and 40-45°C
0.065
formaldehyde
-
XoxF1, in the absence of lanthanides, pH and temperature not specified in the publication
0.066
formaldehyde
at pH 9.0 and 30°C
0.096
formaldehyde
-
XoxF1, in the presence of La3+, pH and temperature not specified in the publication
0.133
formaldehyde
-
XoxF1, in the presence of Nd3+, pH and temperature not specified in the publication
0.432
formaldehyde
-
subtype XoxF4-1, at pH 9.0 and 26°C
0.464
formaldehyde
-
at pH 9.0 and 26°C
0.815
formaldehyde
-
subtype XoxF4-2, at pH 9.0 and 26°C
0.0008
methanol
-
at pH 7.0 and 40-45°C
0.0008
methanol
-
in the presence of a mixture of La3+, Ce3+, Pr3+, Nd3+, at pH 7.2 and 60°C
0.0008
methanol
-
pH and temperature not specified in the publication, lanthanide: Eu3+, Lu3+
0.0008
methanol
-
pH and temperature not specified in the publication, lanthanide: La3+, Ce3+, Pr3+, Nd3+
0.00082
methanol
-
in the presence of 0.02 mM Eu3+ and Lu3+, at pH 7.2 and 45°C
0.0009
methanol
-
pH and temperature not specified in the publication, lanthanide: Eu3+
0.00091
methanol
-
in the presence of 0.02 mM Eu3+, at pH 7.2 and 45°C
0.0013
methanol
-
pH and temperature not specified in the publication, lanthanide: Eu3+, La3+
0.00132
methanol
-
in the presence of 0.02 mM Eu3+ and La3+, at pH 7.2 and 45°C
0.00362
methanol
-
in the presence of 0.02 mM Eu3+, at pH 7.2 and 45°C
0.011
methanol
-
XoxF1, in the absence of lanthanides, pH and temperature not specified in the publication
0.012
methanol
-
pH and temperature not specified in the publication, methanol dehydrogenase XoxF5-2
0.015
methanol
-
pH and temperature not specified in the publication
0.015
methanol
pH and temperature not specified in the publication
0.017
methanol
-
pH and temperature not specified in the publication
0.018
methanol
in the presence of Nd3+, at pH 7.0 and 30°C
0.021
methanol
-
pH and temperature not specified in the publication, methanol dehydrogenase XoxF5-1
0.022
methanol
in the presence of La3+, at pH 7.0 and 30°C
0.023
methanol
-
pH and temperature not specified in the publication
0.024
methanol
-
pH and temperature not specified in the publication
0.029
methanol
-
XoxF1, in the presence of Nd3+, pH and temperature not specified in the publication
0.029
methanol
-
pH and temperature not specified in the publication, lanthanide: Ce3+
0.029
methanol
pH and temperature not specified in the publication, lanthanide: Nd3+
0.03
methanol
-
pH and temperature not specified in the publication
0.039
methanol
-
pH and temperature not specified in the publication
0.039
methanol
-
pH and temperature not specified in the publication, lanthanide: Ce3+
0.039
methanol
-
pH and temperature not specified in the publication, methanol dehydrogenase XoxF4-1
0.042
methanol
-
subtype XoxF4-2, at pH 9.0 and 26°C
0.042
methanol
-
pH and temperature not specified in the publication, methanol dehydrogenase XoxF4-1
0.044
methanol
-
XoxF1, in the presence of La3+, pH and temperature not specified in the publication
0.044
methanol
pH and temperature not specified in the publication, lanthanide: La3+
0.049
methanol
in the presence of Ce3+, at pH 7.0 and 30°C
0.055
methanol
-
subtype XoxF4-1, at pH 9.0 and 26°C
0.055
methanol
-
pH and temperature not specified in the publication, lanthanide: Ce3+
0.067
methanol
-
at pH 9.0 and 30°C
5.98
methanol
at pH 9.0 and 30°C
0.0025
oxidized cytochrome cL
in the presence of La3+, at pH 7.0 and 30°C
-
0.0044
oxidized cytochrome cL
in the presence of Ce3+, at pH 7.0 and 30°C
-
0.0076
oxidized cytochrome cL
in the presence of Nd3+, at pH 7.0 and 30°C
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
when La-, Ce-, and Nd-metalated XoxFs are assayed with XoxG as electron acceptor, the Vmax values are not significantly different for the three enzymes, but the Km for XoxG increases from 0.0025 mM for La-XoxF to 0.0076 mM for Nd-XoxF
-
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evolution
XoxJ are predicted to be members of the periplasmic binding protein (PBP) family
evolution
XoxJ, encoded by the core Ln-MDH operon, is a member of the periplasmic (or solute) binding protein (PBP or SBP) family
evolution
-
XoxJ are predicted to be members of the periplasmic binding protein (PBP) family
-
evolution
-
XoxJ, encoded by the core Ln-MDH operon, is a member of the periplasmic (or solute) binding protein (PBP or SBP) family
-
evolution
-
XoxJ are predicted to be members of the periplasmic binding protein (PBP) family
-
evolution
-
XoxJ, encoded by the core Ln-MDH operon, is a member of the periplasmic (or solute) binding protein (PBP or SBP) family
-
evolution
-
XoxJ are predicted to be members of the periplasmic binding protein (PBP) family
-
evolution
-
XoxJ, encoded by the core Ln-MDH operon, is a member of the periplasmic (or solute) binding protein (PBP or SBP) family
-
evolution
-
XoxJ are predicted to be members of the periplasmic binding protein (PBP) family
-
evolution
-
XoxJ, encoded by the core Ln-MDH operon, is a member of the periplasmic (or solute) binding protein (PBP or SBP) family
-
malfunction
xoxF is required for the expression of mxaF in Methylobacterium aquaticum 22A, since xoxF deletion mutants are not able to grow in the presence of calcium
malfunction
-
xoxF is required for the expression of mxaF in Methylobacterium aquaticum 22A, since xoxF deletion mutants are not able to grow in the presence of calcium
-
metabolism
the enzyme is involved in methanol oxidation. XoxF1 is capable of formaldehyde oxidation in vivo and in vitro and alleviates formaldehyde toxicity in formaldehyde oxidation-pathway mutants but in the absence of the NADH-producing pathways, it cannot solely support methanol growth
metabolism
the enzyme participates in the methanol oxidation pathway
metabolism
xoxF is required for the expression of mxaF in Methylobacterium aquaticum 22A, since xoxF deletion mutants are not able to grow in the presence of calcium
metabolism
XoxF is the preferred enzyme for methanol oxidation, even when calcium is present in 100fold higher concentrations than lanthanide
metabolism
-
xoxF is required for the expression of mxaF in Methylobacterium aquaticum 22A, since xoxF deletion mutants are not able to grow in the presence of calcium
-
metabolism
-
the enzyme is involved in methanol oxidation. XoxF1 is capable of formaldehyde oxidation in vivo and in vitro and alleviates formaldehyde toxicity in formaldehyde oxidation-pathway mutants but in the absence of the NADH-producing pathways, it cannot solely support methanol growth
-
metabolism
-
XoxF is the preferred enzyme for methanol oxidation, even when calcium is present in 100fold higher concentrations than lanthanide
-
physiological function
-
the enzyme contributes to lanthanide-dependent methanol growth
physiological function
lanthanide (Ln)-dependent methanol dehydrogenases (MDHs) have been recently shown to be widespread in methylotrophic bacteria. Along with the core MDH protein, XoxF, these systems comprise two other proteins, XoxG (a c-type cytochrome) and XoxJ (a periplasmic binding protein of unknown function) in methyltroph, Methylobacterium extorquens strain AM1. In contrast to results obtained via an artificial assay system, assays of XoxFs metallated with LaIII, CeIII, and NdIII using their physiological electron acceptor, XoxG, display Ln-independent activities, the Km for XoxG markedly increases from La to Nd. This result suggests that XoxG's redox properties are tuned specifically for lighter Lns in XoxF, an interpretation supported by the unusually low reduction potential of XoxG (+172 mV). The reduction potential of isolated XoxG measured may reasonably approximate the potential of the cytochrome in complex with XoxF
physiological function
-
lanthanoid-dependent methanol dehydrogenase (Eu-MDH) from the acidophilic verrucomicrobial methanotroph Methylacidiphilum fumariolicum SolV has its own physiological cytochrome cGJ electron acceptor. Eu-MDH harbours a redox active 2,7,9-tricarboxypyrroloquinoline quinone (PQQ) cofactor which is non-covalently bound but coordinates trivalent lanthanoid elements including Eu3+. Eu-MDH and the cytochrome are co-adsorbed with the biopolymer chitosan and cast onto a mercaptoundecanol (MU) monolayer modified Au working electrode. Cyclic voltammetry of cytochrome cGJ reveals a well-defined quasi-reversible FeIII/II redox couple at +255 mV versus normal hydrogen electrode (NHE) at pH 7.5, and this response is pH independent. The reversible one-electron response of the cytochrome cGJ transforms into a sigmoidal catalytic wave in the presence of Eu-MDH and its substrates (methanol or formaldehyde). The catalytic current is pH-dependent, and pH 7.3 is optimal
physiological function
-
lanthanoid-dependent methanol dehydrogenase (Eu-MDH) from the acidophilic verrucomicrobial methanotroph Methylacidiphilum fumariolicum SolV has its own physiological cytochrome cGJ electron acceptor. Eu-MDH harbours a redox active 2,7,9-tricarboxypyrroloquinoline quinone (PQQ) cofactor which is non-covalently bound but coordinates trivalent lanthanoid elements including Eu3+. Eu-MDH and the cytochrome are co-adsorbed with the biopolymer chitosan and cast onto a mercaptoundecanol (MU) monolayer modified Au working electrode. Cyclic voltammetry of cytochrome cGJ reveals a well-defined quasi-reversible FeIII/II redox couple at +255 mV versus normal hydrogen electrode (NHE) at pH 7.5, and this response is pH independent. The reversible one-electron response of the cytochrome cGJ transforms into a sigmoidal catalytic wave in the presence of Eu-MDH and its substrates (methanol or formaldehyde). The catalytic current is pH-dependent, and pH 7.3 is optimal
-
physiological function
-
lanthanide (Ln)-dependent methanol dehydrogenases (MDHs) have been recently shown to be widespread in methylotrophic bacteria. Along with the core MDH protein, XoxF, these systems comprise two other proteins, XoxG (a c-type cytochrome) and XoxJ (a periplasmic binding protein of unknown function) in methyltroph, Methylobacterium extorquens strain AM1. In contrast to results obtained via an artificial assay system, assays of XoxFs metallated with LaIII, CeIII, and NdIII using their physiological electron acceptor, XoxG, display Ln-independent activities, the Km for XoxG markedly increases from La to Nd. This result suggests that XoxG's redox properties are tuned specifically for lighter Lns in XoxF, an interpretation supported by the unusually low reduction potential of XoxG (+172 mV). The reduction potential of isolated XoxG measured may reasonably approximate the potential of the cytochrome in complex with XoxF
-
physiological function
-
lanthanide (Ln)-dependent methanol dehydrogenases (MDHs) have been recently shown to be widespread in methylotrophic bacteria. Along with the core MDH protein, XoxF, these systems comprise two other proteins, XoxG (a c-type cytochrome) and XoxJ (a periplasmic binding protein of unknown function) in methyltroph, Methylobacterium extorquens strain AM1. In contrast to results obtained via an artificial assay system, assays of XoxFs metallated with LaIII, CeIII, and NdIII using their physiological electron acceptor, XoxG, display Ln-independent activities, the Km for XoxG markedly increases from La to Nd. This result suggests that XoxG's redox properties are tuned specifically for lighter Lns in XoxF, an interpretation supported by the unusually low reduction potential of XoxG (+172 mV). The reduction potential of isolated XoxG measured may reasonably approximate the potential of the cytochrome in complex with XoxF
-
physiological function
-
lanthanide (Ln)-dependent methanol dehydrogenases (MDHs) have been recently shown to be widespread in methylotrophic bacteria. Along with the core MDH protein, XoxF, these systems comprise two other proteins, XoxG (a c-type cytochrome) and XoxJ (a periplasmic binding protein of unknown function) in methyltroph, Methylobacterium extorquens strain AM1. In contrast to results obtained via an artificial assay system, assays of XoxFs metallated with LaIII, CeIII, and NdIII using their physiological electron acceptor, XoxG, display Ln-independent activities, the Km for XoxG markedly increases from La to Nd. This result suggests that XoxG's redox properties are tuned specifically for lighter Lns in XoxF, an interpretation supported by the unusually low reduction potential of XoxG (+172 mV). The reduction potential of isolated XoxG measured may reasonably approximate the potential of the cytochrome in complex with XoxF
-
physiological function
-
lanthanide (Ln)-dependent methanol dehydrogenases (MDHs) have been recently shown to be widespread in methylotrophic bacteria. Along with the core MDH protein, XoxF, these systems comprise two other proteins, XoxG (a c-type cytochrome) and XoxJ (a periplasmic binding protein of unknown function) in methyltroph, Methylobacterium extorquens strain AM1. In contrast to results obtained via an artificial assay system, assays of XoxFs metallated with LaIII, CeIII, and NdIII using their physiological electron acceptor, XoxG, display Ln-independent activities, the Km for XoxG markedly increases from La to Nd. This result suggests that XoxG's redox properties are tuned specifically for lighter Lns in XoxF, an interpretation supported by the unusually low reduction potential of XoxG (+172 mV). The reduction potential of isolated XoxG measured may reasonably approximate the potential of the cytochrome in complex with XoxF
-
additional information
XoxF is encoded in an operon alongside genes encoding a c-type cytochrome, XoxG, the physiological electron acceptor for XoxF, as well as a periplasmic solute binding protein (SBP) XoxJ. The crystal structure of XoxJ reveals general architectures similar to classic SBPs, except it exhibits an exceptionally large cavity, putatively for substrate binding, as well as a beta-sheet missing several strands
additional information
-
XoxF is encoded in an operon alongside genes encoding a c-type cytochrome, XoxG, the physiological electron acceptor for XoxF, as well as a periplasmic solute binding protein (SBP) XoxJ. The crystal structure of XoxJ reveals general architectures similar to classic SBPs, except it exhibits an exceptionally large cavity, putatively for substrate binding, as well as a beta-sheet missing several strands
-
additional information
-
XoxF is encoded in an operon alongside genes encoding a c-type cytochrome, XoxG, the physiological electron acceptor for XoxF, as well as a periplasmic solute binding protein (SBP) XoxJ. The crystal structure of XoxJ reveals general architectures similar to classic SBPs, except it exhibits an exceptionally large cavity, putatively for substrate binding, as well as a beta-sheet missing several strands
-
additional information
-
XoxF is encoded in an operon alongside genes encoding a c-type cytochrome, XoxG, the physiological electron acceptor for XoxF, as well as a periplasmic solute binding protein (SBP) XoxJ. The crystal structure of XoxJ reveals general architectures similar to classic SBPs, except it exhibits an exceptionally large cavity, putatively for substrate binding, as well as a beta-sheet missing several strands
-
additional information
-
XoxF is encoded in an operon alongside genes encoding a c-type cytochrome, XoxG, the physiological electron acceptor for XoxF, as well as a periplasmic solute binding protein (SBP) XoxJ. The crystal structure of XoxJ reveals general architectures similar to classic SBPs, except it exhibits an exceptionally large cavity, putatively for substrate binding, as well as a beta-sheet missing several strands
-
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Good, N.M.; Vu, H.N.; Suriano, C.J.; Subuyuj, G.A.; Skovran, E.; Martinez-Gomez, N.C.
Pyrroloquinoline quinone ethanol dehydrogenase in Methylobacterium extorquens AM1 extends lanthanide-dependent metabolism to multicarbon substrates
J. Bacteriol.
198
3109-3118
2016
Methylorubrum extorquens (C5AXV8), Methylorubrum extorquens
brenda
Versantvoort, W.; Pol, A.; Daumann, L.J.; Larrabee, J.A.; Strayer, A.H.; Jetten, M.S.M.; van Niftrik, L.; Reimann, J.; Op den Camp, H.J.M.
Characterization of a novel cytochrome cGJ as the electron acceptor of XoxF-MDH in the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV
Biochim. Biophys. Acta Proteins Proteom.
1867
595-603
2019
Methylacidiphilum fumariolicum, Methylacidiphilum fumariolicum SolV
brenda
Featherston, E.R.; Rose, H.R.; McBride, M.J.; Taylor, E.M.; Boal, A.K.; Cotruvo, J.A.
Biochemical and structural characterization of XoxG and XoxJ and their roles in lanthanide-dependent methanol dehydrogenase activity
ChemBioChem
20
2360-2372
2019
Methylorubrum extorquens, Methylorubrum extorquens (P16027 AND P14775 AND P14774), Methylorubrum extorquens NCIMB 9133 (P16027 AND P14775 AND P14774), Methylorubrum extorquens DSM 1338 (P16027 AND P14775 AND P14774), Methylorubrum extorquens ATCC 14718 (P16027 AND P14775 AND P14774), Methylorubrum extorquens JCM 2805 (P16027 AND P14775 AND P14774)
brenda
Bogart, J.A.; Lewis, A.J.; Schelter, E.J.
DFT study of the active site of the XoxF-type natural, cerium-dependent methanol dehydrogenase enzyme
Chemistry
21
1743-1748
2015
Methylacidiphilum fumariolicum, Methylacidiphilum fumariolicum SolV
brenda
Prejano, M.; Marino, T.; Russo, N.
How can methanol dehydrogenase from Methylacidiphilum fumariolicum work with the alien CeIII ion in the active center? A theoretical study
Chemistry
23
8652-8657
2017
Methylacidiphilum fumariolicum
brenda
Lumpe, H.; Pol, A.; Op den Camp, H.J.M.; Daumann, L.J.
Impact of the lanthanide contraction on the activity of a lanthanide-dependent methanol dehydrogenase - a kinetic and DFT study
Dalton Trans.
47
10463-10472
2018
Methylacidiphilum fumariolicum, Methylacidiphilum fumariolicum SolV
brenda
Pol, A.; Barends, T.R.; Dietl, A.; Khadem, A.F.; Eygensteyn, J.; Jetten, M.S.; Op den Camp, H.J.
Rare earth metals are essential for methanotrophic life in volcanic mudpots
Environ. Microbiol.
16
255-264
2014
Methylacidiphilum fumariolicum, Methylacidiphilum fumariolicum SolV
brenda
Lv, H.; Sahin, N.; Tani, A.
Isolation and genomic characterization of Novimethylophilus kurashikiensis gen. nov. sp. nov., a new lanthanide-dependent methylotrophic species of Methylophilaceae
Environ. Microbiol.
20
1204-1223
2018
Novimethylophilus kurashikiensis, Novimethylophilus kurashikiensis La2-4T
brenda
Wang, L.; Suganuma, S.; Hibino, A.; Mitsui, R.; Tani, A.; Matsumoto, T.; Ebihara, A.; Fitriyanto, N.A.; Pertiwiningrum, A.; Shimada, M.; Hayakawa, T.; Nakagawa, T.
Lanthanide-dependent methanol dehydrogenase from the legume symbiotic nitrogen-fixing bacterium Bradyrhizobium diazoefficiens strain USDA110
Enzyme Microb. Technol.
130
109371
2019
Bradyrhizobium diazoefficiens, Bradyrhizobium diazoefficiens USDA110
brenda
Huang, J.; Yu, Z.; Chistoserdova, L.
Lanthanide-dependent methanol dehydrogenases of XoxF4 and XoxF5 clades are differentially distributed among methylotrophic bacteria and they reveal different biochemical properties
Front. Microbiol.
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1366
2018
Methylotenera mobilis, Methylomonas sp. LW13, Methylotenera mobilis JLW8
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De Simone, G.; Polticelli, F.; Aime, S.; Ascenzi, P.
Lanthanides-based catalysis in eukaryotes
IUBMB Life
70
1067-1075
2018
Methylacidiphilum fumariolicum, Methylacidiphilum fumariolicum SolV
brenda
De Simone, G.; Polticelli, F.; Aime, S.; Ascenzi, P.
No lanthanides-based catalysis in eukaryotes
IUBMB Life
71
398-399
2019
no activity in eukaryotes
brenda
McSkimming, A.; Cheisson, T.; Carroll, P.J.; Schelter, E.J.
Functional synthetic model for the lanthanide-dependent quinoid alcohol dehydrogenase active site
J. Am. Chem. Soc.
140
1223-1226
2018
Methylacidiphilum fumariolicum, Methylacidiphilum fumariolicum SoIV
brenda
Vu, H.N.; Subuyuj, G.A.; Vijayakumar, S.; Good, N.M.; Martinez-Gomez, N.C.; Skovran, E.
Lanthanide-dependent regulation of methanol oxidation systems in Methylobacterium extorquens AM1 and their contribution to methanol growth
J. Bacteriol.
198
1250-1259
2016
Methylorubrum extorquens
brenda
Chu, F.; Lidstrom, M.E.
XoxF acts as the predominant methanol dehydrogenase in the type I methanotroph Methylomicrobium buryatense
J. Bacteriol.
198
1317-1325
2016
Methylotuvimicrobium buryatense, Methylotuvimicrobium buryatense 5GB1C
brenda
Deng, Y.W.; Ro, S.Y.; Rosenzweig, A.C.
Structure and function of the lanthanide-dependent methanol dehydrogenase XoxF from the methanotroph Methylomicrobium buryatense 5GB1C
J. Biol. Inorg. Chem.
23
1037-1047
2018
Methylotuvimicrobium buryatense, Methylotuvimicrobium buryatense 5GB1C
brenda
Hibi, Y.; Asai, K.; Arafuka, H.; Hamajima, M.; Iwama, T.; Kawai, K.
Molecular structure of La3+-induced methanol dehydrogenase-like protein in Methylobacterium radiotolerans
J. Biosci. Bioeng.
111
547-549
2011
Methylobacterium radiotolerans, Methylobacterium radiotolerans NBRC15690
brenda
Zheng, Y.; Huang, J.; Zhao, F.; Chistoserdova, L.
Physiological effect of XoxG(4) on lanthanide-dependent methanotrophy
mBio
9
e02430-17
2018
Methylomonas sp. LW13
brenda
Masuda, S.; Suzuki, Y.; Fujitani, Y.; Mitsui, R.; Nakagawa, T.; Shintani, M.; Tani, A.
Lanthanide-dependent regulation of methylotrophy in Methylobacterium aquaticum strain 22A
mSphere
3
e00462-17
2018
Methylobacterium aquaticum, Methylobacterium aquaticum 22A
brenda
Nakagawa, T.; Mitsui, R.; Tani, A.; Sasa, K.; Tashiro, S.; Iwama, T.; Hayakawa, T.; Kawai, K.
A catalytic role of XoxF1 as La3+-dependent methanol dehydrogenase in Methylobacterium extorquens strain AM1
PLoS ONE
7
e50480
2012
Methylorubrum extorquens
brenda
Good, N.M.; Moore, R.S.; Suriano, C.J.; Martinez-Gomez, N.C.
Contrasting in vitro and in vivo methanol oxidation activities of lanthanide-dependent alcohol dehydrogenases XoxF1 and ExaF from Methylobacterium extorquens AM1
Sci. Rep.
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4248
2019
Methylorubrum extorquens
brenda
Versantvoort, W.; Pol, A.; Daumann, L.J.; Larrabee, J.A.; Strayer, A.H.; Jetten, M.S.M.; van Niftrik, L.; Reimann, J.; Op den Camp, H.J.M.
Characterization of a novel cytochrome cGJ as the electron acceptor of XoxF-MDH in the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV
Biochim. Biophys. Acta
1867
595-603
2019
Methylacidiphilum fumariolicum, Methylacidiphilum fumariolicum SolV
brenda
Kalimuthu, P.; Daumann, L.J.; Pol, A.; Op den Camp, H.J.M.; Bernhardt, P.V.
Electrocatalysis of a europium-dependent bacterial methanol dehydrogenase with its physiological electron-acceptor cytochrome cGJ
Chemistry
25
8760-8768
2019
Methylacidiphilum fumariolicum, Methylacidiphilum fumariolicum SolV
brenda
Picone, N.; Op den Camp, H.J.
Role of rare earth elements in methanol oxidation
Curr. Opin. Chem. Biol.
49
39-44
2019
Bradyrhizobium sp., Methylotenera mobilis, Methylacidiphilum fumariolicum, Methylomonas sp. LW13, Methylobacterium aquaticum (A0A0C6F7V8), Methylotuvimicrobium buryatense (A0A3F2YLY8), Methylorubrum extorquens (C5B120), Methylacidiphilum fumariolicum SolV, Methylobacterium aquaticum 22A (A0A0C6F7V8), Methylotuvimicrobium buryatense 5G (A0A3F2YLY8), Methylotenera mobilis JLW8
brenda
Wang, L.; Hibino, A.; Suganuma, S.; Ebihara, A.; Iwamoto, S.; Mitsui, R.; Tani, A.; Shimada, M.; Hayakawa, T.; Nakagawa, T.
Preference for particular lanthanide species and thermal stability of XoxFs in Methylorubrum extorquens strain AM1
Enzyme Microb. Technol.
136
109518
2020
Methylorubrum extorquens (C5B120), Methylorubrum extorquens
brenda
Roszczenko-Jasinska, P.; Krucon, T.; Stasiuk, R.; Matlakowska, R.
Occurrence of XoxF-type methanol dehydrogenases in bacteria inhabiting light lanthanide-rich shale rock
FEMS Microbiol. Ecol.
97
fiaa259
2021
Hyphomicrobium zavarzinii, Methyloferula stellata, Rhodospirillales bacterium, Methyloceanibacter caenitepidi (A0A0A8JZD4), Methyloceanibacter caenitepidi (A0A0A8K0T2), Methyloceanibacter caenitepidi (A0A0A8K4A4), Methyloceanibacter stevinii (A0A1E3VNN9), Paracoccus yeei (A0A1V0GRH2), Methylibium petroleiphilum (A2SLA7), Rhodobacter sp. SW2 (C8S0N8), Candidatus Filomicrobium marinum (CFX30213.1), Hyphomicrobium sp. (F8JBP2), Advenella kashmirensis (I3UDT0), Hyphomicrobium denitrificans (N0B5Z3), Hyphomicrobium denitrificans (N0B8G3), Hyphomicrobium nitrativorans (V5SGT2), Bradyrhizobium sp. (WP 024520589.1), Methylobacterium sp. GXF4 (WP_007560853.1), Methylotenera mobilis (WP_019899159.1), Mesorhizobium sp. LSJC280B00 (X5Q003), Advenella kashmirensis DSM 17095 (I3UDT0), Hyphomicrobium denitrificans 1NES1 (N0B5Z3), Hyphomicrobium denitrificans 1NES1 (N0B8G3), Bradyrhizobium sp. Tv2a-2 (WP 024520589.1), Hyphomicrobium sp. MC1 (F8JBP2), Rhodospirillales bacterium URHD0088, Hyphomicrobium zavarzinii 1NES1, Hyphomicrobium nitrativorans NL23 (V5SGT2)
brenda
Good, N.M.; Fellner, M.; Demirer, K.; Hu, J.; Hausinger, R.P.; Martinez-Gomez, N.C.
Lanthanide-dependent alcohol dehydrogenases require an essential aspartate residue for metal coordination and enzymatic function
J. Biol. Chem.
295
8272-8284
2020
Methylorubrum extorquens (C5B120)
brenda
Jahn, B.; Jonasson, N.S.W.; Hu, H.; Singer, H.; Pol, A.; Good, N.M.; den Camp, H.J.M.O.; Martinez-Gomez, N.C.; Daumann, L.J.
Understanding the chemistry of the artificial electron acceptors PES, PMS, DCPIP and Wursters Blue in methanol dehydrogenase assays
J. Biol. Inorg. Chem.
25
199-212
2020
Methylacidiphilum fumariolicum, Methylorubrum extorquens (C5B120), Methylacidiphilum fumariolicum SolV
brenda
Pastawan, V.; Suganuma, S.; Mizuno, K.; Wang, L.; Tani, A.; Mitsui, R.; Nakamura, K.; Shimada, M.; Hayakawa, T.; Fitriyanto, N.A.; Nakagawa, T.
Regulation of lanthanide-dependent methanol oxidation pathway in the legume symbiotic nitrogen-fixing bacterium Bradyrhizobium sp. strain Ce-3
J. Biosci. Bioeng.
130
582-587
2020
Bradyrhizobium sp. MAFF 211645 (A0A7G1H3Z0)
brenda
Friedman, R.
Preferential binding of lanthanides to methanol dehydrogenase evaluated with density functional theory
J. Phys. Chem. B
125
2251-2257
2021
Methylotuvimicrobium buryatense (A0A3F2YLY8), Methylotuvimicrobium buryatense 5G (A0A3F2YLY8)
brenda
Featherston, E.R.; Mattocks, J.A.; Tirsch, J.L.; Cotruvo, J.A.
Heterologous expression, purification, and characterization of proteins in the lanthanome
Methods Enzymol.
650
119-157
2021
Methylorubrum extorquens (P16027 AND P14775 AND P14774), Methylorubrum extorquens NCIMB 9133 (P16027 AND P14775 AND P14774), Methylorubrum extorquens DSM 1338 (P16027 AND P14775 AND P14774), Methylorubrum extorquens ATCC 14718 (P16027 AND P14775 AND P14774), Methylorubrum extorquens JCM 2805 (P16027 AND P14775 AND P14774)
brenda
Huang, J.; Zheng, Y.; Groom, J.; Yu, Z.; Chistoserdova, L.
Expression, purification and properties of the enzymes involved in lanthanide-dependent alcohol oxidation XoxF4, XoxF5, ExaF/PedH, and XoxG4
Methods Enzymol.
650
81-96
2021
Methylorubrum extorquens, Sinorhizobium meliloti, Bradyrhizobium diazoefficiens, Methylotenera mobilis, Methylomonas sp. LW13, Grimontia marina, Rhodovulum kholense, Tistlia consotensis, Methyloversatilis discipulorum (B2LME2), Bradyrhizobium diazoefficiens USDA 110, Sinorhizobium meliloti 5A14, Grimontia marina CECT 8713, Methyloversatilis discipulorum FAM1 (B2LME2), Methylotenera mobilis JLW8, Tistlia consotensis DSM 21585, Rhodovulum kholense DSM 19783
brenda
Yanpirat, P.; Nakatsuji, Y.; Hiraga, S.; Fujitani, Y.; Izumi, T.; Masuda, S.; Mitsui, R.; Nakagawa, T.; Tani, A.
Lanthanide-dependent methanol and formaldehyde oxidation in Methylobacterium aquaticum strain 22A
Microorganisms
8
822
2020
Methylobacterium aquaticum (A0A0C6F7V8), Methylobacterium aquaticum, Methylobacterium aquaticum 22A (A0A0C6F7V8)
brenda