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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
-
methanotrophic
- methane
-
pyrroloquinoline
- quinone
- formaldehyde
-
earth
- pqq
-
methylacidiphilum
-
fumariolicum
-
extorquens
- lanthanum
-
methylobacterium
-
methylotrophy
-
pqq-dependent
-
mxafis
-
rare-earth
- neodymium
-
ceiii
-
quinoproteins
-
methylorubrum
- methylophilaceae
- buryatense
The expected taxonomic range for this enzyme is: Bacteria
Reaction Schemes
+
2
oxidized cytochrome cL
=
+
2
reduced cytochrome cL
Synonyms
xoxf1, xoxf5, xoxf-type methanol dehydrogenase, eu-mdh, xoxf-type mdh, ce-mdh, xoxf-mdh, lanthanide-dependent mdh, lanthanide-dependent methanol dehydrogenase, ln-dependent ethanol dehydrogenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ce-MDH
Ce3+-dependent XoxF1-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
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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 oxidized cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
?
methanol + 2 oxidized cytochrome cGJ
formaldehyde + 2 reduced cytochrome cGJ
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ce3+
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
La3+
Nd3+
Pr3+
Sm3+
additional information
Ce3+
-
highest activity with 0.03 mM Ce3+. The enzyme contains 0.58 cerium atoms per subunit
La3+
-
between 0 and 0.005 mM La3+ a sharp increase in enzyme activity is observed
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
Nd3+
-
between 0 and 0.005 mM La3+ a sharp increase in enzyme activity is observed
Pr3+
-
between 0 and 0.005 mM La3+ a sharp increase in enzyme activity is observed
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
-
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.014
ethanol
-
XoxF1, in the absence of lanthanides, pH and temperature not specified in the publication
0.067
ethanol
-
XoxF1, in the presence of La3+, 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
0.133
formaldehyde
-
XoxF1, in the presence of Nd3+, 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
0.00082
methanol
-
in the presence of 0.02 mM Eu3+ and Lu3+, at pH 7.2 and 45°C
0.00091
methanol
-
in the presence of 0.02 mM Eu3+, 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
0.011
methanol
-
XoxF1, in the absence of lanthanides, 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
0.044
methanol
-
XoxF1, in the presence of La3+, pH and temperature not specified in the publication
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
-
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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
3
methanol
-
XoxF1, in the absence of lanthanides, 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
55
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
210
methanol
-
XoxF1, in the presence of Nd3+, 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
-
the enzyme contributes to lanthanide-dependent methanol growth
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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
-
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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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
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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
Methylomicrobium buryatense, Methylomicrobium buryatense 5GB1C
brenda
Hibi, Y.; Asai, K.; Arafuka, H.; Hamajima, M.; Iwama, T.; Kawai, K.
Molecular structure of La3+-induced methanol dehydrogenase-like protein in Methylobacterium radiotolerans
J. Biosci. Bioeng.
111
547-549
2011
Methylobacterium radiotolerans, Methylobacterium radiotolerans NBRC15690
brenda
Zheng, Y.; Huang, J.; Zhao, F.; Chistoserdova, L.
Physiological effect of XoxG(4) on lanthanide-dependent methanotrophy
mBio
9
e02430-17
2018
Methylomonas sp. LW13
brenda
Masuda, S.; Suzuki, Y.; Fujitani, Y.; Mitsui, R.; Nakagawa, T.; Shintani, M.; Tani, A.
Lanthanide-dependent regulation of methylotrophy in Methylobacterium aquaticum strain 22A
mSphere
3
e00462-17
2018
Methylobacterium aquaticum, Methylobacterium aquaticum 22A
brenda
Nakagawa, T.; Mitsui, R.; Tani, A.; Sasa, K.; Tashiro, S.; Iwama, T.; Hayakawa, T.; Kawai, K.
A catalytic role of XoxF1 as La3+-dependent methanol dehydrogenase in Methylobacterium extorquens strain AM1
PLoS ONE
7
e50480
2012
Methylorubrum extorquens
brenda
Good, N.M.; Moore, R.S.; Suriano, C.J.; Martinez-Gomez, N.C.
Contrasting in vitro and in vivo methanol oxidation activities of lanthanide-dependent alcohol dehydrogenases XoxF1 and ExaF from Methylobacterium extorquens AM1
Sci. Rep.
9
4248
2019
Methylorubrum extorquens
brenda
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