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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
-
Substrates: 100% activity compared to methanol
Products: -
?
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
-
Substrates: less than 50% activity compared to methanol
Products: -
?
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 cL
formaldehyde + 2 reduced cytochrome cL
methanol + oxidized cytochrome c XoxG
formaldehyde + reduced cytochrome c XoxG
-
Substrates: -
Products: -
?
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
-
Substrates: 78.3% activity compared to methanol
Products: -
r
1-butanol + phenazine ethosulfate
butyraldehyde + reduced phenazine ethosulfate
-
Substrates: 78.3% activity compared to methanol
Products: -
r
1-butanol + phenazine ethosulfate
butyraldehyde + reduced phenazine ethosulfate
-
Substrates: 100% activity compared to methanol
Products: -
?
1-butanol + phenazine methosulfate

butyraldehyde + reduced phenazine methosulfate
-
Substrates: more than 95% activity compared to methanol
Products: -
r
1-butanol + phenazine methosulfate
butyraldehyde + reduced phenazine methosulfate
-
Substrates: more than 95% activity compared to methanol
Products: -
r
1-hexanol + phenazine methosulfate

hexaldehyde + reduced phenazine methosulfate
-
Substrates: more than 95% activity compared to methanol
Products: -
r
1-hexanol + phenazine methosulfate
hexaldehyde + reduced phenazine methosulfate
-
Substrates: more than 95% activity compared to methanol
Products: -
r
1-propanol + phenazine ethosulfate

propionaldehyde + reduced phenazine ethosulfate
-
Substrates: 85.3% activity compared to methanol
Products: -
r
1-propanol + phenazine ethosulfate
propionaldehyde + reduced phenazine ethosulfate
-
Substrates: 85.3% activity compared to methanol
Products: -
r
1-propanol + phenazine ethosulfate
propionaldehyde + reduced phenazine ethosulfate
-
Substrates: 100% activity compared to methanol
Products: -
?
1-propanol + phenazine ethosulfate
propionaldehyde + reduced phenazine ethosulfate
-
Substrates: 100% activity compared to methanol
Products: -
?
1-propanol + phenazine methosulfate

propionaldehyde + reduced phenazine methosulfate
-
Substrates: more than 95% activity compared to methanol
Products: -
r
1-propanol + phenazine methosulfate
propionaldehyde + reduced phenazine methosulfate
-
Substrates: more than 95% activity compared to methanol
Products: -
r
1-propanol + phenazine methosulfate
propionaldehyde + reduced phenazine methosulfate
-
Substrates: more than 95% activity compared to methanol
Products: -
r
2-propanol + phenazine ethosulfate

?
-
Substrates: 0.775% activity compared to methanol
Products: -
r
2-propanol + phenazine ethosulfate
?
-
Substrates: 0.775% activity compared to methanol
Products: -
r
2-propanol + phenazine methosulfate

?
-
Substrates: 40% activity compared to methanol
Products: -
r
2-propanol + phenazine methosulfate
?
-
Substrates: subtype XoxF4-1 shows 20% activity compared to methanol, subtype XoxF4-2 shows 5% activity compared to methanol
Products: -
r
2-propanol + phenazine methosulfate
?
-
Substrates: subtype XoxF4-1 shows 20% activity compared to methanol, subtype XoxF4-2 shows 5% activity compared to methanol
Products: -
r
acetaldehyde + reduced phenazine methosulfate

ethanol + phenazine methosulfate
-
Substrates: 60% activity compared to methanol
Products: -
r
acetaldehyde + reduced phenazine methosulfate
ethanol + phenazine methosulfate
-
Substrates: subtype XoxF4-1 shows 50% activity compared to methanol, subtype XoxF4-2 shows 15% activity compared to methanol
Products: -
r
ethanol + phenazine ethosulfate

acetaldehyde + reduced phenazine ethosulfate
-
Substrates: 93% activity compared to methanol
Products: -
r
ethanol + phenazine ethosulfate
acetaldehyde + reduced phenazine ethosulfate
-
Substrates: 93% activity compared to methanol
Products: -
r
ethanol + phenazine ethosulfate
acetaldehyde + reduced phenazine ethosulfate
-
Substrates: 100% activity compared to methanol
Products: -
?
ethanol + phenazine ethosulfate
acetaldehyde + reduced phenazine ethosulfate
-
Substrates: 100% activity compared to methanol
Products: -
?
ethanol + phenazine methosulfate

acetaldehyde + reduced phenazine methosulfate
-
Substrates: more than 95% activity compared to methanol
Products: -
r
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
Substrates: highest activity
Products: -
r
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
-
Substrates: best substrate for ExaF
Products: -
?
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
-
Substrates: more than 95% activity compared to methanol
Products: -
r
ethanol + phenazine methosulfate
acetaldehyde + reduced phenazine methosulfate
-
Substrates: more than 95% activity compared to methanol
Products: -
r
formaldehyde + phenazine methosulfate + ?

formate + reduced phenazine methosulfate + ?
Substrates: -
Products: -
?
formaldehyde + phenazine methosulfate + ?
formate + reduced phenazine methosulfate + ?
Substrates: -
Products: -
?
formaldehyde + reduced phenazine ethosulfate

methanol + phenazine ethosulfate
-
Substrates: 91.5% activity compared to methanol
Products: -
r
formaldehyde + reduced phenazine ethosulfate
methanol + phenazine ethosulfate
-
Substrates: 100% activity compared to methanol
Products: -
r
formaldehyde + reduced phenazine methosulfate

methanol + phenazine methosulfate
-
Substrates: more than 95% activity compared to methanol
Products: -
r
formaldehyde + reduced phenazine methosulfate
methanol + phenazine methosulfate
Substrates: the enzyme is 100times more efficient at oxidizing formaldehyde than methanol
Products: -
r
formaldehyde + reduced phenazine methosulfate
methanol + phenazine methosulfate
-
Substrates: more than 95% activity compared to methanol
Products: -
r
formaldehyde + reduced phenazine methosulfate
methanol + phenazine methosulfate
-
Substrates: more than 95% activity compared to methanol
Products: -
r
methanol + 2 cytochrome cGJ

formaldehyde + 2 reduced cytochrome cGJ
-
Substrates: -
Products: -
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
Substrates: 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
Products: -
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
Substrates: electrochemical redox reaction
Products: -
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
Substrates: -
Products: -
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
Substrates: 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
Products: -
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
Substrates: -
Products: -
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
Substrates: electrochemical redox reaction
Products: -
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
Substrates: -
Products: -
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
Substrates: -
Products: -
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
Substrates: -
Products: -
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
Substrates: -
Products: -
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
Substrates: -
Products: -
r
methanol + 2 oxidized cytochrome cL

formaldehyde + 2 reduced cytochrome cL
-
Substrates: -
Products: -
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
Substrates: -
Products: -
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
Substrates: c-type cytochrome XoxG
Products: -
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
Substrates: -
Products: -
?
methanol + phenazine ethosulfate

formaldehyde + reduced phenazine ethosulfate
-
Substrates: 100% activity
Products: -
r
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
-
Substrates: 100% activity
Products: -
r
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
-
Substrates: -
Products: -
?
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
-
Substrates: 100% activity
Products: -
r
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
-
Substrates: -
Products: -
?
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
-
Substrates: -
Products: -
?
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
-
Substrates: 100% activity
Products: -
r
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
-
Substrates: -
Products: -
?
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
Substrates: -
Products: -
?
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
Substrates: -
Products: -
?
methanol + phenazine methosulfate

formaldehyde + reduced phenazine ethosulfate
-
Substrates: methanol is the preferred substrate
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine ethosulfate
-
Substrates: methanol is the preferred substrate
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine ethosulfate
-
Substrates: methanol is the preferred substrate
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine ethosulfate
-
Substrates: methanol is the preferred substrate
Products: -
?
methanol + phenazine methosulfate

formaldehyde + reduced phenazine methosulfate
-
Substrates: methanol is the preferred substrate
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: methanol is the preferred substrate
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: 100% activity
Products: -
r
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: 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
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: 100% activity
Products: -
r
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: 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
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: 100% activity
Products: -
r
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: methanol is the preferred substrate
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
Substrates: -
Products: -
r
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: best substrate for XoxF1
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
Substrates: 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
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: methanol is the preferred substrate
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: 100% activity
Products: -
r
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: methanol is the preferred substrate
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: 100% activity
Products: -
r
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: methanol is the preferred substrate
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: -
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
Substrates: methanol is the preferred substrate
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
Substrates: methanol is the preferred substrate
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: methanol is the preferred substrate
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: methanol is the preferred substrate
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: methanol is the preferred substrate
Products: -
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
Substrates: methanol is the preferred substrate
Products: -
?
methanol + Wurster's Blue

formaldehyde + ?
-
Substrates: 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
Products: -
?
methanol + Wurster's Blue
formaldehyde + ?
-
Substrates: 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
Products: -
?
methanol + Wurster's Blue
formaldehyde + ?
Substrates: 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
Products: -
?
propionaldehyde + reduced phenazine methosulfate

1-propanol + phenazine methosulfate
-
Substrates: 60% activity compared to methanol
Products: -
r
propionaldehyde + reduced phenazine methosulfate
1-propanol + phenazine methosulfate
-
Substrates: subtype XoxF4-1 shows 50% activity compared to methanol, subtype XoxF4-2 shows 15% activity compared to methanol
Products: -
r
additional information

?
-
-
Substrates: no activity with 2-propanol and formate
Products: -
?
additional information
?
-
-
Substrates: no activity with 2-propanol and formate
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
additional information
?
-
Substrates: 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
Products: -
?
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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+
-
between 0 and 0.005 mM La3+ a sharp increase in enzyme activity is observed
La3+
-
lanthanide-dependent enzyme
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+
-
the enzyme is activated by La3+. The purified enzyme contains 0.91 atoms of La3+ atoms per dimer
La3+
-
dependent on. XoxF1 contains La3+ in 1:1 molar ratio of metal to protomer
La3+
-
lanthanide-dependent enzyme
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+
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+
a lanthanide is required
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+
-
between 0 and 0.005 mM La3+ a sharp increase in enzyme activity is observed
Nd3+
-
lanthanide-dependent enzyme
Nd3+
-
lanthanide-dependent enzyme
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+
a lanthanide is required
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
-
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
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
-
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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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
-
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 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
-
physiological function

-
the enzyme contributes to lanthanide-dependent methanol growth
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
-
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
-
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
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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 ATCC 14718 (P16027 AND P14775 AND P14774), Methylorubrum extorquens DSM 1338 (P16027 AND P14775 AND P14774), Methylorubrum extorquens JCM 2805 (P16027 AND P14775 AND P14774), Methylorubrum extorquens NCIMB 9133 (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
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2015
Candidatus Methylacidiphilum fumarolicum, Candidatus Methylacidiphilum fumarolicum 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
Candidatus Methylacidiphilum fumarolicum
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
Candidatus Methylacidiphilum fumarolicum, Candidatus Methylacidiphilum fumarolicum 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
Candidatus Methylacidiphilum fumarolicum, Candidatus Methylacidiphilum fumarolicum 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.
9
1366
2018
Methylomonas sp. LW13, Methylotenera mobilis, Methylotenera mobilis JLW8
brenda
De Simone, G.; Polticelli, F.; Aime, S.; Ascenzi, P.
Lanthanides-based catalysis in eukaryotes
IUBMB Life
70
1067-1075
2018
Candidatus Methylacidiphilum fumarolicum, Candidatus Methylacidiphilum fumarolicum 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
Candidatus Methylacidiphilum fumarolicum, Candidatus Methylacidiphilum fumarolicum 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
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2016
Methylorubrum extorquens
brenda
Chu, F.; Lidstrom, M.E.
XoxF acts as the predominant methanol dehydrogenase in the type I methanotroph Methylomicrobium buryatense
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198
1317-1325
2016
Methylotuvimicrobium buryatense, Methylotuvimicrobium buryatense 5GB1C
brenda
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Structure and function of the lanthanide-dependent methanol dehydrogenase XoxF from the methanotroph Methylomicrobium buryatense 5GB1C
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23
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2018
Methylotuvimicrobium buryatense, Methylotuvimicrobium buryatense 5GB1C
brenda
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Molecular structure of La3+-induced methanol dehydrogenase-like protein in Methylobacterium radiotolerans
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2011
Methylobacterium radiotolerans, Methylobacterium radiotolerans NBRC15690
brenda
Zheng, Y.; Huang, J.; Zhao, F.; Chistoserdova, L.
Physiological effect of XoxG(4) on lanthanide-dependent methanotrophy
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9
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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
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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
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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.
9
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
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1867
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2019
Candidatus Methylacidiphilum fumarolicum, Candidatus Methylacidiphilum fumarolicum 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
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Candidatus Methylacidiphilum fumarolicum, Candidatus Methylacidiphilum fumarolicum SolV
brenda
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Role of rare earth elements in methanol oxidation
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49
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2019
Bradyrhizobium sp., Candidatus Methylacidiphilum fumarolicum, Candidatus Methylacidiphilum fumarolicum SolV, Methylobacterium aquaticum (A0A0C6F7V8), Methylobacterium aquaticum 22A (A0A0C6F7V8), Methylomonas sp. LW13, Methylorubrum extorquens (C5B120), Methylotenera mobilis, Methylotenera mobilis JLW8, Methylotuvimicrobium buryatense (A0A3F2YLY8), Methylotuvimicrobium buryatense 5G (A0A3F2YLY8)
brenda
Wang, L.; Hibino, A.; Suganuma, S.; Ebihara, A.; Iwamoto, S.; Mitsui, R.; Tani, A.; Shimada, M.; Hayakawa, T.; Nakagawa, T.
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136
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Methylorubrum extorquens (C5B120), Methylorubrum extorquens
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Roszczenko-Jasinska, P.; Krucon, T.; Stasiuk, R.; Matlakowska, R.
Occurrence of XoxF-type methanol dehydrogenases in bacteria inhabiting light lanthanide-rich shale rock
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97
fiaa259
2021
Advenella kashmirensis (I3UDT0), Advenella kashmirensis DSM 17095 (I3UDT0), Bradyrhizobium sp. (WP 024520589.1), Bradyrhizobium sp. Tv2a-2 (WP 024520589.1), Candidatus Filomicrobium marinum (CFX30213.1), Hyphomicrobium denitrificans (N0B8G3), Hyphomicrobium denitrificans (N0B5Z3), Hyphomicrobium denitrificans 1NES1 (N0B8G3), Hyphomicrobium denitrificans 1NES1 (N0B5Z3), Hyphomicrobium nitrativorans (V5SGT2), Hyphomicrobium nitrativorans NL23 (V5SGT2), Hyphomicrobium sp. (F8JBP2), Hyphomicrobium sp. MC1 (F8JBP2), Hyphomicrobium zavarzinii, Hyphomicrobium zavarzinii 1NES1, Mesorhizobium sp. LSJC280B00 (X5Q003), Methylibium petroleiphilum (A2SLA7), Methylobacterium sp. GXF4 (WP_007560853.1), Methyloceanibacter caenitepidi (A0A0A8JZD4), Methyloceanibacter caenitepidi (A0A0A8K0T2), Methyloceanibacter caenitepidi (A0A0A8K4A4), Methyloceanibacter stevinii (A0A1E3VNN9), Methyloferula stellata, Methylotenera mobilis (WP_019899159.1), Paracoccus yeei (A0A1V0GRH2), Rhodobacter ferrooxidans (C8S0N8), Rhodospirillales bacterium, Rhodospirillales bacterium URHD0088
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
Candidatus Methylacidiphilum fumarolicum, Candidatus Methylacidiphilum fumarolicum SolV, Methylorubrum extorquens (C5B120)
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 ATCC 14718 (P16027 AND P14775 AND P14774), Methylorubrum extorquens DSM 1338 (P16027 AND P14775 AND P14774), Methylorubrum extorquens JCM 2805 (P16027 AND P14775 AND P14774), Methylorubrum extorquens NCIMB 9133 (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
Bradyrhizobium diazoefficiens, Bradyrhizobium diazoefficiens USDA 110, Grimontia marina, Grimontia marina CECT 8713, Methylomonas sp. LW13, Methylorubrum extorquens, Methylotenera mobilis, Methylotenera mobilis JLW8, Methyloversatilis discipulorum (B2LME2), Methyloversatilis discipulorum FAM1 (B2LME2), Rhodovulum kholense, Rhodovulum kholense DSM 19783, Sinorhizobium meliloti, Sinorhizobium meliloti 5A14, Tistlia consotensis, Tistlia consotensis DSM 21585
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