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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 + reduced phenazine ethosulfate
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine methosulfate
methanol + phenazine methosulfate
methanol + 2 oxidized cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
c-type cytochrome XoxG
-
-
?
methanol + oxidized cytochrome c XoxG
formaldehyde + reduced cytochrome c XoxG
-
-
-
-
?
methanol + phenazine ethosulfate
formaldehyde + reduced phenazine ethosulfate
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
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-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-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
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 + 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 oxidized cytochrome cGJ

formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
?
methanol + 2 oxidized cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
?
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 methosulfate

formaldehyde + reduced phenazine methosulfate
-
100% activity
-
-
r
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 + 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 + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
-
-
r
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
best substrate for XoxF1
-
-
?
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
100% activity
-
-
r
methanol + phenazine methosulfate
formaldehyde + reduced phenazine methosulfate
-
100% activity
-
-
r
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
additional information

?
-
-
no activity with 2-propanol and formate
-
-
-
additional information
?
-
-
no activity with 2-propanol and formate
-
-
-
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2,7,9-tricarboxypyrroloquinoline quinone
-
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+
cytochrome cGJ

-
-
-
cytochrome cGJ
-
c-type cytochrome, XoxG, contains a heme-binding pocket. Recombinant expression in Escherichia coli strain BL21(DE3) and purification from periplasm, method overview. 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. Determination of extinction coefficients and redox potential
-
cytochrome cGJ
-
encoded by gene Mfumv2_1185, the cytochrome cL homologue from the strictly lanthanide-dependent, thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV is a fusion of a XoxG cytochrome and a periplasmic binding protein XoxJ. XoxGJ functions as the direct electron acceptor of its corresponding XoxF-type MDH and can sustain methanol turnover, when a secondary cytochrome is present as final electron acceptor. SolV cytochrome cGJ (XoxGJ) further displays a unique, red-shifted absorbance spectrum, with a Soret and Q bands at 440, 553 and 595 nm in the reduced state, respectively. VTVH-MCD spectroscopy reveals the presence of a low spin iron heme and the data further shows that the heme group exhibits minimal ruffling. The midpoint potential Em,pH7 of +240 mV is similar to other cytochrome cL type proteins but the midpoint potential of cytochrome cGJ is not influenced by lowering the pH. Covalently attached heme c moiety, the heme modification of SolV cytochrome cGJ, might stabilize it at lower pH and prevent the increase in midpoint potential
-
cytochrome cGJ
-
XoxG exhibits an unusually low reduction potential with impact on physiological methanol oxidation, XoxG crystal structure and structure-function analysis. The heme c moiety, which is covalently attached to the protein through two thioether bonds to C95 and C98 via the signature CXXCH motif for heme attachment, is enclosed in a hydrophobic pocket formed by three core alpha-helices (helices I, III, and V). This binding motif leaves one of the heme edges open to solvent. Typical of most class I c-type cytochromes, the FeIII is axially ligated by a His residue contributed by helix I (H99) and a Met residue from the loop between helices III and V (M143). Unlike most other class I cytochromes c, XoxG lacks helix IV, and this region is instead a 19-residue loop, the end of which is partially disordered. Alignment of XoxG with the cytochrome c domain and the XoxF homology model with the dehydrogenase domain suggests a plausible XoxF binding interface on XoxG. In the model, the loops between helices I and II and between III and V in XoxG are positioned to interact with XoxF. The X-ray crystal structure of XoxG is solved to 2.71 A resolution
-
pyrroloquinoline quinone

-
-
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-
-
pyrroloquinoline quinone
-
PQQ, PQQ is synthesized in the cytosol, but the proteins that use it are periplasmic, it might bind to subunit XoxJ near or at residue W200, no binding to XoxJ mutant W200F. Metal-bound PQQ is bound at subunit XoxF
pyrroloquinoline quinone
-
PQQ, recombinant expression and binding analysis, method overview
pyrroloquinoline quinone
-
pyrroloquinoline quinone-containing enzyme
pyrroloquinoline quinone
-
pyrroloquinoline quinone-containing enzyme
pyrroloquinoline quinone
-
pyrroloquinoline quinone-containing enzyme
pyrroloquinoline quinone
-
pyrroloquinoline quinone-containing enzyme
pyrroloquinoline quinone
-
pyrroloquinoline quinone-containing enzyme
pyrroloquinoline quinone
-
pyrroloquinoline quinone-containing enzyme
pyrroloquinoline quinone
-
pyrroloquinoline quinone-containing enzyme
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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. 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. 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
-
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
-
0.096
1-butanol

-
at pH 9.0 and 26°C
0.006
1-butanol
-
at pH 7.0 and 40-45°C
0.47
1-butanol
-
subtype XoxF4-2, at pH 9.0 and 26°C
0.188
1-butanol
-
subtype XoxF4-1, at pH 9.0 and 26°C
0.002
1-Hexanol

-
at pH 7.0 and 40-45°C
0.04
1-Hexanol
-
at pH 9.0 and 26°C
0.037
1-Hexanol
-
subtype XoxF4-1, at pH 9.0 and 26°C
0.357
1-Hexanol
-
subtype XoxF4-2, at pH 9.0 and 26°C
0.133
1-propanol

-
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
0.873
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
0.067
ethanol
-
XoxF1, in the presence of La3+, pH and temperature not specified in the publication
0.014
ethanol
-
XoxF1, in the absence of lanthanides, pH and temperature not specified in the publication
0.085
ethanol
-
at pH 9.0 and 26°C
0.059
ethanol
-
subtype XoxF4-1, at pH 9.0 and 26°C
0.515
ethanol
-
subtype XoxF4-2, at pH 9.0 and 26°C
0.133
formaldehyde

-
XoxF1, in the presence of Nd3+, pH and temperature not specified in the publication
0.065
formaldehyde
-
XoxF1, in the absence of lanthanides, pH and temperature not specified in the publication
0.007
formaldehyde
-
at pH 7.0 and 40-45°C
0.096
formaldehyde
-
XoxF1, in the presence of La3+, pH and temperature not specified in the publication
0.066
formaldehyde
at pH 9.0 and 30°C
0.432
formaldehyde
-
subtype XoxF4-1, at pH 9.0 and 26°C
0.815
formaldehyde
-
subtype XoxF4-2, at pH 9.0 and 26°C
0.464
formaldehyde
-
at pH 9.0 and 26°C
0.03
methanol

-
pH and temperature not specified in the publication
0.0009
methanol
-
pH and temperature not specified in the publication, lanthanide: Eu3+
0.012
methanol
-
pH and temperature not specified in the publication, methanol dehydrogenase XoxF5-2
0.049
methanol
-
in the presence of Ce3+, at pH 7.0 and 30°C
0.015
methanol
-
pH and temperature not specified in the publication
0.015
methanol
-
pH and temperature not specified in the publication
0.018
methanol
-
in the presence of Nd3+, at pH 7.0 and 30°C
0.022
methanol
-
in the presence of La3+, at pH 7.0 and 30°C
0.021
methanol
-
pH and temperature not specified in the publication, methanol dehydrogenase XoxF5-1
0.023
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+
0.067
methanol
-
at pH 9.0 and 30°C
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
0.011
methanol
-
XoxF1, in the absence of lanthanides, pH and temperature not specified in the publication
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+
0.055
methanol
-
subtype XoxF4-1, at pH 9.0 and 26°C
0.055
methanol
-
pH and temperature not specified in the publication, lanthanide: Ce3+
0.017
methanol
-
pH and temperature not specified in the publication
0.0013
methanol
-
pH and temperature not specified in the publication, lanthanide: Eu3+, La3+
0.024
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
0.044
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+
0.00091
methanol
-
in the presence of 0.02 mM Eu3+, at pH 7.2 and 45°C
0.00082
methanol
-
in the presence of 0.02 mM Eu3+ and Lu3+, at pH 7.2 and 45°C
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
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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20
acetaldehyde
at pH 9.0 and 30°C
170 - 490
oxidized cytochrome cL
-
2.15
1-butanol

-
subtype XoxF4-2, at pH 9.0 and 26°C
16.63
1-butanol
-
subtype XoxF4-1, at pH 9.0 and 26°C
133.9
1-butanol
-
at pH 9.0 and 26°C
5.54
1-Hexanol

-
subtype XoxF4-2, at pH 9.0 and 26°C
34.88
1-Hexanol
-
subtype XoxF4-1, at pH 9.0 and 26°C
415.52
1-Hexanol
-
at pH 9.0 and 26°C
1.73
1-propanol

-
subtype XoxF4-2, at pH 9.0 and 26°C
35.36
1-propanol
-
subtype XoxF4-1, at pH 9.0 and 26°C
112.54
1-propanol
-
at pH 9.0 and 26°C
4
ethanol

-
XoxF1, in the absence of lanthanides, pH and temperature not specified in the publication
194
ethanol
-
XoxF1, in the presence of La3+, pH and temperature not specified in the publication
14500
ethanol
at pH 9.0 and 30°C
5.99
ethanol
-
subtype XoxF4-2, at pH 9.0 and 26°C
27.03
ethanol
-
subtype XoxF4-1, at pH 9.0 and 26°C
159.15
ethanol
-
at pH 9.0 and 26°C
5
formaldehyde

-
XoxF1, in the absence of lanthanides, pH and temperature not specified in the publication
36
formaldehyde
-
XoxF1, in the presence of Nd3+, pH and temperature not specified in the publication
109
formaldehyde
-
XoxF1, in the presence of La3+, pH and temperature not specified in the publication
259
formaldehyde
at pH 9.0 and 30°C
2.48
formaldehyde
-
subtype XoxF4-2, at pH 9.0 and 26°C
3.97
formaldehyde
-
subtype XoxF4-1, at pH 9.0 and 26°C
37.86
formaldehyde
-
at pH 9.0 and 26°C
210
methanol

-
XoxF1, in the presence of Nd3+, pH and temperature not specified in the publication
26
methanol
-
in the presence of 0.02 mM Eu3+ and Lu3+, at pH 7.2 and 45°C
50
methanol
-
in the presence of 0.02 mM Eu3+, at pH 7.2 and 45°C
2
methanol
at pH 9.0 and 30°C
67
methanol
-
in the presence of Nd3+, at pH 7.0 and 30°C
190
methanol
-
in the presence of La3+, at pH 7.0 and 30°C
123
methanol
-
in the presence of 0.02 mM Eu3+ and La3+, at pH 7.2 and 45°C
55
methanol
-
in the presence of 0.02 mM Eu3+, at pH 7.2 and 45°C
3
methanol
-
XoxF1, in the absence of lanthanides, pH and temperature not specified in the publication
57
methanol
-
in the presence of Ce3+, at pH 7.0 and 30°C
272
methanol
-
XoxF1, in the presence of La3+, pH and temperature not specified in the publication
5800
methanol
-
in the presence of a mixture of La3+, Ce3+, Pr3+, Nd3+, at pH 7.2 and 60°C
27.17
methanol
-
subtype XoxF4-1, at pH 9.0 and 26°C
42.19
methanol
-
subtype XoxF4-2, at pH 9.0 and 26°C
342.55
methanol
-
at pH 9.0 and 26°C
170
oxidized cytochrome cL

-
in the presence of Nd3+, at pH 7.0 and 30°C
-
280
oxidized cytochrome cL
-
in the presence of Ce3+, at pH 7.0 and 30°C
-
490
oxidized cytochrome cL
-
in the presence of La3+, at pH 7.0 and 30°C
-
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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
-
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
-
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
-
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
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
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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
Methylotenera mobilis, Methylomonas sp. LW13, Methylotenera mobilis JLW8
brenda
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
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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.
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2016
Methylorubrum extorquens
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Chu, F.; Lidstrom, M.E.
XoxF acts as the predominant methanol dehydrogenase in the type I methanotroph Methylomicrobium buryatense
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198
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2016
Methylomicrobium buryatense, Methylomicrobium buryatense 5GB1C
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Structure and function of the lanthanide-dependent methanol dehydrogenase XoxF from the methanotroph Methylomicrobium buryatense 5GB1C
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2018
Methylomicrobium buryatense, Methylomicrobium buryatense 5GB1C
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Molecular structure of La3+-induced methanol dehydrogenase-like protein in Methylobacterium radiotolerans
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111
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2011
Methylobacterium radiotolerans, Methylobacterium radiotolerans NBRC15690
brenda
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Physiological effect of XoxG(4) on lanthanide-dependent methanotrophy
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Methylomonas sp. LW13
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Lanthanide-dependent regulation of methylotrophy in Methylobacterium aquaticum strain 22A
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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
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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
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4248
2019
Methylorubrum extorquens
brenda