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Information on EC 1.1.2.10 - lanthanide-dependent methanol dehydrogenase
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1.1.2.10 lanthanide-dependent methanol dehydrogenaseIUBMB Comments
Isolated from the bacterium Methylacidiphilum fumariolicum and many Methylobacterium species. Requires La3+, Ce3+, Pr3+ or Nd3+. The higher lanthanides show decreasing activity with Sm3+, Eu3+ and Gd3+. The lanthanide is coordinated by the enzyme and pyrroloquinoline quinone. Shows little activity with Ca2+, the required cofactor of EC 1.1.2.7, methanol dehydrogenase (cytochrome c).
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Word Map
- 1.1.2.10
-
xoxfs
- methanotrophs
- methane
- formaldehyde
-
pyrroloquinoline
- extorquens
- fumariolicum
-
methylotrophy
- lanthanum
- methylobacterium
- methylacidiphilum
- pqq
-
pqq-dependent
-
mxafis
-
rare-earth
-
methylorubrum
-
volcanic
- neodymium
-
methane-utilizing
-
ceiii
- buryatense
-
praseodymium
-
quinoproteins
-
verrucomicrobial
-
geothermal
- methylophilaceae
The expected taxonomic range for this enzyme is: Bacteria
Reaction Schemes
+
2
oxidized cytochrome cL
=
+
2
reduced cytochrome cL
Synonyms
Ce-MDH, Ce-XoxF, Ce3+-dependent XoxF1-MDH, Ce3+-induced methanol dehydrogenase, cerium dependent MDH, cerium-dependent methanol dehydrogenase, Eu-MDH, exaF, La-XoxF, La2+-MDH-like protein, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ce-MDH
Ce3+-dependent XoxF1-MDH
Ce3+-induced methanol dehydrogenase
-
-
-
-
cerium dependent MDH
-
-
-
-
cerium-dependent methanol dehydrogenase
Eu-MDH
exaF
La2+-MDH-like protein
La3+-dependent MDH
La3+-induced methanol dehydrogenase-like protein
lanthanide-dependent alcohol dehydrogenase
lanthanide-dependent MDH
lanthanide-dependent quinoid alcohol dehydrogenase
lanthanide-dependent XoxF-type methanol dehydrogenase
lanthanidedependent XoxF-MDH
lanthanides-dependent MDH
Ln-dependent MDH
Ln-MDH
methanol dehydrogenase
XoxF
XoxF dehydrogenase
XoxF methanol dehydrogenase
XoxF-MDH
XoxF-type MDH
xoxF1
XoxF4-1
XoxF4-2
XoxF5-type MDH
XoxFMDH
Ce-MDH
-
-
-
-
La3+-dependent MDH
-
-
-
-
XoxF
-
-
-
-
XoxF-MDH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
methanol + 2 oxidized cytochrome cL = formaldehyde + 2 reduced cytochrome cL
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
methanol:cytochrome cL oxidoreductase
Isolated from the bacterium Methylacidiphilum fumariolicum and many Methylobacterium species. Requires La3+, Ce3+, Pr3+ or Nd3+. The higher lanthanides show decreasing activity with Sm3+, Eu3+ and Gd3+. The lanthanide is coordinated by the enzyme and pyrroloquinoline quinone. Shows little activity with Ca2+, the required cofactor of EC 1.1.2.7, methanol dehydrogenase (cytochrome c).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetaldehyde + reduced phenazine ethosulfate
ethanol + phenazine ethosulfate
-
less than 50% activity compared to methanol
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
c-type cytochrome XoxG
-
-
?
methanol + oxidized cytochrome c XoxG
formaldehyde + reduced cytochrome c XoxG
-
-
-
-
?
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
methanol + oxidized cytochrome c XoxG
formaldehyde + reduced cytochrome c XoxG
-
-
-
-
?
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
r
methanol + 2 cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
r
methanol + 2 oxidized cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
?
methanol + 2 oxidized cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
-
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ce3+
Dy3+
Eu3+
Gd3+
La3+
Lu3+
Nd3+
Pr3+
Sm3+
additional information
Ce3+
-
highest activity with 0.03 mM Ce3+. The enzyme contains 0.58 cerium atoms per subunit
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+
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
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+
-
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+
-
lanthanides are an essential cofactor for XoxF-type methanol dehydrogenases
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+
-
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+
-
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. 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+)
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+
-
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. 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
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
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
-
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ammonia
-
ammonia reveals a slight inhibitory effect on subtype XoxF4-2
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.133
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
0.096
formaldehyde
-
XoxF1, in the presence of La3+, 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
0.015
methanol
-
pH and temperature not specified in the publication
0.015
methanol
-
pH and temperature not specified in the publication
0.021
methanol
-
pH and temperature not specified in the publication, methanol dehydrogenase XoxF5-1
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+
0.042
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
-
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
-
pH and temperature not specified in the publication, lanthanide: Ce3+
0.0013
methanol
-
pH and temperature not specified in the publication, lanthanide: Eu3+, La3+
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
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
oxidized cytochrome cL
-
in the presence of Ce3+, at pH 7.0 and 30°C
-
1.2
oxidized cytochrome cL
-
in the presence of La3+, at pH 7.0 and 30°C
-
1.3
oxidized cytochrome cL
-
in the presence of Nd3+, at pH 7.0 and 30°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
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
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
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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 9.5
-
the enzyme shows more than 50% activity between pH 7.5 and 9.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
metabolism
evolution
additional information
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). C5AXV8_METEA
Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)
587
0
63767
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 22% (w/v) PEG 8000, 0.2 M NaCl
-
crystal structures of XoxF1, one with and another without pyrroloquinoline quinone, both with La3+x02 bound in the active-site region and coordinated by Asp320
-
purified wild-type XoxJ, X-ray diffraction structure determination and analysis at 2.27 A resolution, single-wavelength anomalous diffraction method, molecular replacement method and modeling, soaking of PQQ into XoxJ crystals is unsuccessful
-
sitting drop vapor diffusion method, using 0.2 M magnesium acetate, 0.1 M sodium cacodylate, pH 6.5, and 20% (w/v) PEG 8000
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D320A
-
mutant enzyme does not bind La3+. Asp320 is needed for in vivo catalytic function, in vitro activity, and La3+x02 coordination
W200F
W200F
-
site directed mutagenesis, the variant of XoxJ does not bind cofactor PQQ in contrast to the wild-type enzyme
W200F
-
site directed mutagenesis, the variant of XoxJ does not bind cofactor PQQ in contrast to the wild-type enzyme
-
W200F
-
site directed mutagenesis, the variant of XoxJ does not bind cofactor PQQ in contrast to the wild-type enzyme
-
W200F
-
site directed mutagenesis, the variant of XoxJ does not bind cofactor PQQ in contrast to the wild-type enzyme
-
W200F
-
site directed mutagenesis, the variant of XoxJ does not bind cofactor PQQ in contrast to the wild-type enzyme
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-25°C, the enzyme loses approximately 50% of its activity within 24 h whether maintained, on ice, in pH 8.0, pH 8.5, or pH 9.0 Tris buffer supplemented with dithiothreitol and glycerol
0-25°C, the enzyme loses approximately 50% of its activity within 24 h whether maintained, on ice, in pH 8.0, pH 8.5, or pH 9.0 Tris buffer supplemented with dithiothreitol and glycerol
-
0-25°C, the enzyme loses approximately 50% of its activity within 24 h whether maintained, on ice, in pH 8.0, pH 8.5, or pH 9.0 Tris buffer supplemented with dithiothreitol and glycerol
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Toyopearl butyl-650S column chromatography and HiTrap column chromatography
-
Hi-Trap SP HP Sepharose column chromatography and Mono S column chromatography
-
HiTrap SP Sepharose column chromatography and Mono S column chromatography
-
Ni-NTA agarose column chromatography
Source 15Q anion exchange column chromatography and Superdex S200 gel filtration
-
SP Sepharose column chromatography and Superdex 75 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Methylobacterium extorquens AM1
expression Methylobacterium extorquens AM1
gene xoxF, recombinant enzyme expression in Methylorubrum extorquens strain AM1 and in Escherichia coli. gene xoxJ, recombinant expression in Escherichia coli strain BL21(DE3)
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
overexpression of xoxF at higher calcium concentrations compared to lanthanides
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
1223-1226
2018
Methylacidiphilum fumariolicum, Methylacidiphilum fumariolicum SoIV
brenda
Vu, H.N.; Subuyuj, G.A.; Vijayakumar, S.; Good, N.M.; Martinez-Gomez, N.C.; Skovran, E.
Lanthanide-dependent regulation of methanol oxidation systems in Methylobacterium extorquens AM1 and their contribution to methanol growth
J. Bacteriol.
198
1250-1259
2016
Methylorubrum extorquens
brenda
Chu, F.; Lidstrom, M.E.
XoxF acts as the predominant methanol dehydrogenase in the type I methanotroph Methylomicrobium buryatense
J. Bacteriol.
198
1317-1325
2016
Methylomicrobium buryatense, Methylomicrobium buryatense 5GB1C
brenda
Deng, Y.W.; Ro, S.Y.; Rosenzweig, A.C.
Structure and function of the lanthanide-dependent methanol dehydrogenase XoxF from the methanotroph Methylomicrobium buryatense 5GB1C
J. Biol. Inorg. Chem.
23
1037-1047
2018
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Hibi, Y.; Asai, K.; Arafuka, H.; Hamajima, M.; Iwama, T.; Kawai, K.
Molecular structure of La3+-induced methanol dehydrogenase-like protein in Methylobacterium radiotolerans
J. Biosci. Bioeng.
111
547-549
2011
Methylobacterium radiotolerans, Methylobacterium radiotolerans NBRC15690
brenda
Zheng, Y.; Huang, J.; Zhao, F.; Chistoserdova, L.
Physiological effect of XoxG(4) on lanthanide-dependent methanotrophy
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2018
Methylomonas sp. LW13
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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
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2018
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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
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e50480
2012
Methylorubrum extorquens
brenda
Good, N.M.; Moore, R.S.; Suriano, C.J.; Martinez-Gomez, N.C.
Contrasting in vitro and in vivo methanol oxidation activities of lanthanide-dependent alcohol dehydrogenases XoxF1 and ExaF from Methylobacterium extorquens AM1
Sci. Rep.
9
4248
2019
Methylorubrum extorquens
brenda
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