Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
active site structure with bound cofactor, the reduced pyrroloquinoline quinone (PQQ) transfers two electrons in single electron-transfer steps to cytochrome cL, creating a semiquinone form of the prosthetic group after the first electron transfer, electron transfer via enzyme residues Cys104, Asp105, and Asn52
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
additionelimination mechanism and hydride transfer mechanism, the catalytic mechanism, with a tetrahedral intermediate, involves the quinone containing prosthetic group, substrate binding and active site structures, overview, the oxygen atoms of the PQQ are involved in several hydrogen bonds with the residues Glu55, Arg109, Thr153, Ser168, Arg324 and Asn387
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
detailed mechanism of methanol oxidation involving residues Asp297 and Glu171, structure-activity analysis by quantum mechanics and molecular mechanics, QM/MM, selfconsistent-charge density-functional tight-binding, SCC-DFTB, and molecular dynamics, the transition state involves Glu171-CO2- as general base
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
the amino-acid residues related to the active site of MDH, E55, C103, C104, R109, T159, S174, E177, T243, W243, N261, D303, R331, N394, and W476, are completely conserved
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
catalytic mechanism, ping-pong kinetic schemes, and transition state structures, analysis by ab initio quantum mechanical methods, hydride transfer from the Calpha-position of the substrate alcohol or aldehyde directly to the C-5 carbon of PQQ is energetically feasible, detailed overview
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
detailed reaction mechanism with direct hydride transfe, Glu177 plays the role of general base catalyst
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
detailed reaction mechanism with direct hydride transfer
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
chemical structure of pyrroloquinoline quinone and hydride transfer mechanism of the enzymatic reaction catalyzed by MEDH, overview
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
Diplococcus sp.
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
the amino-acid residues related to the active site of MDH, E55, C103, C104, R109, T159, S174, E177, T243, W243, N261, D303, R331, N394, and W476, are completely conserved
-
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
mechanism of methanol oxidation by QMDH, overview
-
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
additionelimination mechanism and hydride transfer mechanism, the catalytic mechanism, with a tetrahedral intermediate, involves the quinone containing prosthetic group, substrate binding and active site structures, overview, the oxygen atoms of the PQQ are involved in several hydrogen bonds with the residues Glu55, Arg109, Thr153, Ser168, Arg324 and Asn387
-
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
chemical structure of pyrroloquinoline quinone and hydride transfer mechanism of the enzymatic reaction catalyzed by MEDH, overview
-
-
a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a primary alcohol + 2 ferricytochrome cL
an aldehyde + 2 ferrocytochrome cL + 2 H+
acetaldehyde + 2 reduced cytochrome cL
ethanol + 2 oxidizeded cytochrome cL
-
7.06% of the activity with methanol
-
-
?
butanol + 2 oxidized cytochrome cL
butanal + 2 reduced cytochrome cL
-
49.13% of the activity with methanol
-
-
?
butanol + 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
ethanol + 2 oxidized cytochrome cL
acetaldehyde + 2 reduced cytochrome cL
-
85.13% of the activity with methanol
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
formaldehyde + 2 reduced cytochrome cL
methanol + 2 oxidizeded cytochrome cL
-
73.24% of the activity with methanol
-
-
?
heptanol + 2 oxidized cytochrome cL
heptanal + 2 reduced cytochrome cL
-
101.88% of the activity with methanol
-
-
?
heptanol + 2,6-dichlorophenolindophenol
heptaldehyde + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
hexanol + 2 oxidized cytochrome cL
hexanal + 2 reduced cytochrome cL
-
94.10% of the activity with methanol
-
-
?
hexanol + 2,6-dichlorophenolindophenol
hexaldehyde + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
methanol + 2 2,6-dichlorophenolindophenol
formaldehyde + 2 reduced 2,6-dichlorophenolindophenol
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
methanol + 2,6-dichlorophenolindophenol
formaldehyde + reduced 2,6-dichlorophenolindophenol
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
methanol + NAD+
formaldehyde + NADH + H+
-
strains grow on methanol
-
-
?
n-butanol + 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
n-propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
octanol + 2 oxidized cytochrome cL
octanal + 2 reduced cytochrome cL
-
16.33% of the activity with methanol
-
-
?
octanol + 2,6-dichlorophenolindophenol
octaldehyde + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
pentanol + 2 oxidized cytochrome cL
pentanal + 2 reduced cytochrome cL
-
67.40% of the activity with methanol
-
-
?
pentanol + 2,6-dichlorophenolindophenol
pentaldehyde + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
propanol + 2 oxidized cytochrome cL
propionaldehyde + 2 reduced cytochrome cL
-
59.93% of the activity with methanol
-
-
?
propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
sorbic alcohol + 2,6-dichlorophenolindophenol
? + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
additional information
?
-
a primary alcohol + 2 ferricytochrome cL
an aldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
?
a primary alcohol + 2 ferricytochrome cL
an aldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
ethanol + 2,6-dichlorophenolindophenol
acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
methanol + 2 2,6-dichlorophenolindophenol
formaldehyde + 2 reduced 2,6-dichlorophenolindophenol
in the activity assay phenazine ethosulfate is used as primary electron acceptor, and 2,6-dichlorophenol indophenol as a terminal acceptor
-
-
?
methanol + 2 2,6-dichlorophenolindophenol
formaldehyde + 2 reduced 2,6-dichlorophenolindophenol
in the activity assay phenazine ethosulfate is used as primary electron acceptor, and 2,6-dichlorophenolindophenol as a terminal acceptor
-
-
?
methanol + 2 2,6-dichlorophenolindophenol
formaldehyde + 2 reduced 2,6-dichlorophenolindophenol
in the activity assay phenazine ethosulfate is used as primary electron acceptor, and 2,6-dichlorophenol indophenol as a terminal acceptor
-
-
?
methanol + 2 2,6-dichlorophenolindophenol
formaldehyde + 2 reduced 2,6-dichlorophenolindophenol
in the activity assay phenazine ethosulfate is used as primary electron acceptor, and 2,6-dichlorophenolindophenol as a terminal acceptor
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
native enzyme with pyrroloquinoline quinone as a prosthetic group and cytochrome cL as the primary electron acceptor
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
native enzyme with pyrroloquinoline quinone as a prosthetic group and cytochrome cL as the primary electron acceptor
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
Diplococcus sp.
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
Diplococcus sp.
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor. Paracoccus denitrificans contains constitutive cytochrome cL, but synthesis of cytochromes c551i and c553i is induced while growing on methanol, structures, overview
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
way of electron transfer from methanol to O2, overview
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
way of electron transfer from methanol to O2, overview
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
-
?
methanol + 2,6-dichlorophenolindophenol
formaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
methanol + 2,6-dichlorophenolindophenol
formaldehyde + reduced 2,6-dichlorophenolindophenol
-
with phenazine methosulfate
-
-
?
methanol + 2,6-dichlorophenolindophenol
formaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
methanol + 2,6-dichlorophenolindophenol
formaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
-
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
-
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
-
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
MDH catalyses the first reaction of an unusual periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria during growth on methane or methanol
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria: methanol, methanol dehydrogenase, cytochrome cL, cytochrome cH, oxidase, oxygen
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
terminal electron acceptor is cytochrome cL
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
MDH catalyses the first reaction of an unusual periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria during growth on methane or methanol
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
the reaction includes an electron transfer from the quinol PQQH2 to the electron acceptor cytochrome CL mediated by the disulfide structure of the active site, the active site of MDH involves Trp243 that forms the base of the active site chamber, and the Cys103-Cys104 disulfide ring and the pyrroloquinoline quinone prosthetic group, which is in the semiquinone form having the oxygen of the C4 carbonyl displaced out of the plane of the ring, overview
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria: methanol, methanol dehydrogenase, cytochrome cL, cytochrome cH, oxidase, oxygen
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
the physiological electron acceptor is cytochrome cL. Cytochrome cL is subsequently oxidized by the small class I c-type cytochrome cH
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
the reaction includes an electron transfer from the quinol PQQH2 to the electron acceptor cytochrome CL mediated by the disulfide structure of the active site, the active site of MDH involves Trp243 that forms the base of the active site chamber, and the Cys103-Cys104 disulfide ring and the pyrroloquinoline quinone prosthetic group, which is in the semiquinone form having the oxygen of the C4 carbonyl displaced out of the plane of the ring, overview
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
-
-
-
?
n-butanol + 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
n-butanol + 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
n-butanol + 2,6-dichlorophenolindophenol
butyraldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
n-propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
n-propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
n-propanol + 2,6-dichlorophenolindophenol
propionaldehyde + reduced 2,6-dichlorophenolindophenol
-
reduction of the acceptor 2,6-dichlorophenolindophenol is mediated by phenazine methosulfate
-
-
?
additional information
?
-
Diplococcus sp.
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
additional information
?
-
-
methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria
-
-
?
additional information
?
-
oxidation of alcohols by direct hydride transfer to the pyrroloquinoline quinone cofactor, catalytic mechanism, ping-pong kinetic schemes, and transition state structures, analysis by ab initio quantum mechanical methods, hydride transfer from the Calpha-position of the substrate alcohol or aldehyde directly to the C-5 carbon of PQQ is energetically feasible, detailed overview
-
-
?
additional information
?
-
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
additional information
?
-
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
additional information
?
-
active site structure with important disulfide bridge of Cys103-Cys104, overview
-
-
?
additional information
?
-
active site structure, the Cys103-Cys104 disulfide bridge plays a role in the electron transfer during catalysis, overview
-
-
?
additional information
?
-
MDH is a soluble periplasmic enzyme, having cytochrome CL as electron acceptor, Ca2+ plays a role in maintaining PQQ in the correct configuration and may also be involved in the catalytic mechanism, overview
-
-
?
additional information
?
-
oxidation of alcohols by direct hydride transfer to the pyrroloquinoline quinone cofactor
-
-
?
additional information
?
-
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
additional information
?
-
-
broad substrate specificity, MDH from Methylosinus sp. strain WI 14 oxidises only primary alcohols up to octanol and several aldehydes
-
-
?
additional information
?
-
-
broad substrate specificity, MDH from Methylosinus sp. strain WI 14 oxidises only primary alcohols up to octanol and several aldehydes
-
-
?
additional information
?
-
-
methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria
-
-
?
additional information
?
-
-
methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria
-
-
?
additional information
?
-
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
additional information
?
-
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
additional information
?
-
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
additional information
?
-
-
1,6-dichlorophenolindophenol, N,N,N',N'-tetramethyl-4-phenylenediamine, and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfuric acid) can act as artificial electron acceptors. The artificial electron acceptors cannot be directly reduced by the enzyme. Their reduction requires the presence of phenazine ethosulfate or phenazine methosulfate. Electrons are transferred from an oxidizing substrate to the PQQ moiety, and protons are released into the cytoplasm. The reduced PQQ moiety donates electrons to cytochrome c one after the other, yielding the semiquinone form of PQQ
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a primary alcohol + 2 ferricytochrome cL
an aldehyde + 2 ferrocytochrome cL + 2 H+
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
additional information
?
-
a primary alcohol + 2 ferricytochrome cL
an aldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
?
a primary alcohol + 2 ferricytochrome cL
an aldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
Diplococcus sp.
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor. Paracoccus denitrificans contains constitutive cytochrome cL, but synthesis of cytochromes c551i and c553i is induced while growing on methanol, structures, overview
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 ferricytochrome cL
formaldehyde + 2 ferrocytochrome cL + 2 H+
-
cytochrome c is the natural electron acceptor
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
way of electron transfer from methanol to O2, overview
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
way of electron transfer from methanol to O2, overview
-
-
?
methanol + 2 oxidized cytochrome cL
formaldehyde + 2 reduced cytochrome cL
-
-
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
-
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
-
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
MDH catalyses the first reaction of an unusual periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria during growth on methane or methanol
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria: methanol, methanol dehydrogenase, cytochrome cL, cytochrome cH, oxidase, oxygen
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
MDH catalyses the first reaction of an unusual periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria during growth on methane or methanol
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
periplasmic electron transport chain responsible for oxidation of methanol to formaldehyde in methylotrophic bacteria: methanol, methanol dehydrogenase, cytochrome cL, cytochrome cH, oxidase, oxygen
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
the physiological electron acceptor is cytochrome cL. Cytochrome cL is subsequently oxidized by the small class I c-type cytochrome cH
-
-
?
methanol + ferricytochrome cL
formaldehyde + ferrocytochrome cL
-
-
-
-
?
additional information
?
-
-
methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria
-
-
?
additional information
?
-
MDH is a soluble periplasmic enzyme, having cytochrome CL as electron acceptor, Ca2+ plays a role in maintaining PQQ in the correct configuration and may also be involved in the catalytic mechanism, overview
-
-
?
additional information
?
-
-
methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria
-
-
?
additional information
?
-
-
methanol dehydrogenase is a key enzyme in utilization of methane and methanol by methylotrophic proteobacteria
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,7,9-tricarboxypyrroloquinoline quinone
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure, overview
cytochrome cL
-
-
-
cytochrome cL
electron acceptor
-
cytochrome cL
flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding and crystal structure determination and analysis at 1.6 A resolution, contains a disulfide bridge that tethers the long C-terminal extension to the body of the structure, overview
-
cytochrome cL
Ma-CytcL, contains heme c and has unique features compared to those of the terrestrial homologues. Apart from Fe2+ in heme, three additional metal ion binding sites for Na+, Ca2+, and Fe2+ are found, wherein the ions mostly form coordination bonds with the amino acid residues on the loop (G93-Y111) that interacts with heme. These ions seem to enhance the stability of heme insertion by increasing the loop's steadiness. The basic N-terminal end, together with helix alpha4 and loop G126-Y136, contributes positive charge to the region. In contrast, the acidic C-terminal end provides a negatively charged surface, yielding several electrostatic contact points with partner proteins for electron transfer. The need for an adapter protein bridging MDH to CytcL within appropriate proximity for electron transfer is satisfied by protein MxaJ. Native Ma-CytcL is purified from Methylophaga aminisulfidivorans cell culture by anion exchange chromatography and gel filtration. It contains a signal peptide, sequence comparisons and metal binding sites analysis, overview
-
cytochrome cL
UniProt ID A3FJ50
-
heme c
part of cytochrome cL
heme c
coordination in CtcL at the active site, structure, overview. Contains Fe2+
phenazine methosulfate
-
mediates reduction of 2,6-dichlorophenol-indophenol
phenazine methosulfate
-
mediates reduction of 2,6-dichlorophenolindophenol
pyrroloquinoline quinone
-
pyrroloquinoline quinone
-
pyrroloquinoline quinone
-
pyrroloquinoline quinone
-
dependent on
pyrroloquinoline quinone
-
dependent on
pyrroloquinoline quinone
-
bound to the enzyme, preparation of Ca2+-free MDH, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, overview
pyrroloquinoline quinone
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound to the active site, 1 molecule per alpha-subunit, required for catalytic activity
pyrroloquinoline quinone
-
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-f]quinoline-2,7,9-tricarboxylaic acid, enzyme-bound, required for catalytic activity, the cofactor is located in a cavity near to the end of an A strand, and it is sandwiched between the indole ring of the residue Trp237 and the S-S bridge of the couple Cys103-Cys104
pyrroloquinoline quinone
PQQ
pyrroloquinoline quinone
PQQ
pyrroloquinoline quinone
-
the enzyme is a type II PQQ-containing alcohol dehydrogenase, the cofactor is bound to the active site in an entirely planar conformation of the tricyclic PQQ cofactor ring, binding structure overview
pyrroloquinoline quinone
binding structure in the active site, overview
pyrroloquinoline quinone
dependent on, prosthetic group, the PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond. One of the carbonyl oxygens of PQQ is bonded to the Ca2+ , probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group
pyrroloquinoline quinone
flow of electrons from reduced pyrroloquinoline quinone to the heme of cytochrome cL, binding structure
pyrroloquinoline quinone
i.e. 2,7,9-tricarboxy-1H-pyrrolo[2,3-f]quinoline-4,5-dione, PQQ, structures of anionic PQQ, neutral PQQ, and reduced PQQ, overview
pyrroloquinoline quinone
i.e. 2,7,9-tricarboxy-1H-pyrrolo[2,3-f]quinoline-4,5-dione, PQQ, structures of anionic PQQ, neutral PQQ, and reduced PQQ, overview
pyrroloquinoline quinone
PQQ, binding structure at the active site, overview, the active site contains a single Ca2 + ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261
pyrroloquinoline quinone
-
PQQ, is the only prosthetic group
pyrroloquinoline quinone
PQQ, prosthetic group
pyrroloquinoline quinone
-
PQQ, serves as the redox cofactor in bacterial MEDH, PQQ is located in a central channel of the disk-shaped protein, and is sandwiched between a Trp side chain and a very unusual vicinal disulfide, binding structure, overview
pyrroloquinoline quinone
PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure at the active site, ab initio structures of 2,7,9-tricarboxypyrroloquinoline quinone, semiquinone, and dihydroquinone, free and in complex with Ca2+, overview
pyrroloquinoline quinone
-
prosthetic group, 1.3 molecules per enzyme molecule
pyrroloquinoline quinone
-
enzyme contains two semiquinone pyrroloquinoline quinone groups per heterotetramer
pyrroloquinoline quinone
PQQ, 2 mol of PQQ per mol of enzyme, the cofactor is predominantly in the semiquinone form, binding structure, overview
pyrroloquinoline quinone
-
PQQ, binding structure at the active site
pyrroloquinoline quinone
PQQ, is the only prosthetic group, the PQQ is sandwiched between the indole ring of Trp243 and the disulfide ring structure, overview
pyrroloquinoline quinone
PQQ, one molecule per enzyme alpha-subunit. The PQQ ring is sandwiched between the indole ring of Trp243 and the two sulphur atoms of the disulfide ring structure
pyrroloquinoline quinone
the pyrroloquinoline quinone prosthetic group is located in the central channel of the large subunit near the surface of the molecule
pyrroloquinoline quinone
-
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
pyrroloquinoline quinone
-
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
pyrroloquinoline quinone
-
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
pyrroloquinoline quinone
-
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
pyrroloquinoline quinone
-
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
pyrroloquinoline quinone
-
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
pyrroloquinoline quinone
Diplococcus sp.
-
i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid, essentially required, binding structure
pyrroloquinoline quinone
the enzyme contains the prosthetic group pyrroloquinoline quinone, PQQ, non-covalently bound, which catalyzes the oxidation of methanol to formaldehyde, two molecules per enzyme tetramer, chemical structure and configuration change of PQQ., overview
pyrroloquinoline quinone
PQQ, active site bound
additional information
an NAD(P)-independent enzyme
-
additional information
an NAD(P)-independent enzyme
-
additional information
Ma-MxaJ contains the bi-lobate folding architecture found in periplasmic binding proteins (PDB ID 5SV6), presence of an acidic cavity at the interface of the two domains
-
additional information
MxaJ, a chaperone-like protein facilitating the assembly of MDH, additional component MxaJ together with a MDHI can facilitate the methanol oxidation process
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Na+
binds to cofactor CytcL, binding site analysis
Sr2+
Ca2+ can be replaced in the incorporation process by strontium or barium, the affinities for these ions being similar to that for Ca2+, Sr2+ shows 94% of the activity with Ca2+
additional information
-
Mg2+ cannot substitute for Ca2+
Ba2+
can substitute for Ca2+, Ba-MDH has twice the maximum activity of the Ca-MDH but with a much lower affinity for its substrates
Ba2+
Ca2+ can be replaced in the incorporation process by strontium or barium, the affinities for these ions being similar to that for Ca2+, Ba2+ shows 102% of the activity with Ca2+
Ba2+
-
modeling of Ba2+-containing MDH active site to investigate the proposed addition-elimination and hydride-transfer methanol oxidation mechanisms. For both mechanisms, almost all the free-energy barriers associated with all of the steps are reduced in the presence of Ba2+-MDH, and they are kinetically feasible. The free energy barriers for methanol oxidation by Ba2+-MDH, particularly for the rate-limiting steps of both mechanisms, are almost half the corresponding barriers calculated for the case of Ca2+-MDH
Ca2+
Diplococcus sp.
-
active site of QMDH contains one Ca2+ ion, removal of Ca2+ ions results in the loss of the enzyme activity, important role of Ca2+ in the catalysis
Ca2+
-
absolutely required, 1.43 Ca2+ per enzyme tetramer, tightly bound to the active site, preparation of Ca2+-free MDH, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, overview, Ca2+-free enzyme is inactive
Ca2+
catalytic, active site-bound
Ca2+
binds to cofactor CytcL, binding site analysis
Ca2+
required for activity
Ca2+
-
required for catalytic activity, binding structure, overview
Ca2+
required for activity, functional role analysis, overview
Ca2+
required for activity, overview
Ca2+
-
active site of QMDH contains one Ca2+ ion, removal of Ca2+ ions results in the loss of the enzyme activity, important role of Ca2+ in the catalysis
Ca2+
two Ca2+ ions per enzyme tetramer, essential for the enzymatic activity
Ca2+
-
binding structure at the active site, overview
Ca2+
-
Ca2+ is six-coordinated with bonds to 05, N6, and carboxyl oxygen 07A of PQQ, the two carboxyl oxygen atoms of Glu171, and the side-chain oxygen of Asn255, binding structure, overview
Ca2+
-
the active site contains a single Ca2+ whose coordination sphere contains PQQ and protein atoms
Ca2+
bound to the active site, required for catalytic activity
Ca2+
-
required, bound at the active site, interaction with the cofactor and the active site residues Arg331, Asp303, and Glu177, but not Asn261, structure overview
Ca2+
binding structure at the active site, overview, the active site contains a single Ca2+ ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261
Ca2+
binding strucure in the active site, overview
Ca2+
one molecule per enzyme alpha-subunit, binding involves Glu177 and Asn261, Ca2+ plays a role in maintaining PQQ in the correct configuration and may also be involved in the catalytic mechanism
Ca2+
required for activity, functional role analysis, overview
Ca2+
the active site contains a single Ca2+ whose coordination sphere contains PQQ and protein atoms
Ca2+
tightly bound close to the inner heme propionate, Ca2+ is involved in stabilization of the redox potential, and is important in the flow of electrons from reduced pyrroloquinoline quinone in methanol dehydrogenase to the heme of cytochrome cL
Ca2+
2 Ca2+ ions are irreversibly incorporated per alpha2beta2 tetramer. Calcium can be replaced in the incorporation process by strontium or barium, the affinities for these ions being similar to that for Ca2+
Ca2+
one molecule of Ca2+ per enzyme tetramer. Ca2+ is directly or indirectly involved in the biding of pyrroloquinoline quinone. Methanol oxidation mutants MoxA-, K- and L- contain no Ca2+. The MoxA, K and L proteins may be involved in maintaining a high Ca2+ concentration in the periplasm. It is more likely, that they fill a chaperone function, stabilizing a configuration of methanol dehydrogenase which permits incorporation of low concentrations of Ca2+ into the protein
Ca2+
one molecule per enzyme alpha-subunit. Neither the quinone form of pyrroloquinoline quinone, nor the disulfide ring or its reduced form are absolutely essential for calcium incorporation into the active site
Ca2+
required for activity, one of the carbonyl oxygens of PQQ is bonded to the Ca2+, probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group
Ca2+
-
active site of QMDH contains one Ca2+ ion, removal of Ca2+ ions results in the loss of the enzyme activity, important role of Ca2+ in the catalysis
Ca2+
-
active site of QMDH contains one Ca2+ ion, removal of Ca2+ ions results in the loss of the enzyme activity, important role of Ca2+ in the catalysis
Ca2+
-
active site of QMDH contains one Ca2+ ion, removal of Ca2+ ions results in the loss of the enzyme activity, important role of Ca2+ in the catalysis
Ca2+
-
active site of QMDH contains one Ca2+ ion, removal of Ca2+ ions results in the loss of the enzyme activity, important role of Ca2+ in the catalysis
Ca2+
-
active site of QMDH contains one Ca2+ ion, removal of Ca2+ ions results in the loss of the enzyme activity, important role of Ca2+ in the catalysis
Fe2+
in heme c, which is contained in cofactor cytochrome cL, and bound to CytcL, binding sites analysis
Fe2+
a cytochrome protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
x * 62000, alpha-subunit, + x * 7500, beta-subunit, SDS-PAGE
?
-
x * 62000, alpha-subunit, + x * 7500, beta-subunit, SDS-PAGE
-
dimer
-
2 * 70000, SDS-PAGE
dimer
-
2 * 70000, SDS-PAGE
-
heterotetramer
alpha2beta2, the MEDH heterotetramer is composed of two large subunits and two small subunits
heterotetramer
-
alpha2beta2, the MEDH heterotetramer is composed of two large subunits and two small subunits
-
heterotetramer
alpha2beta2, the MEDH heterotetramer is composed of two large subunits and two small subunits
heterotetramer
-
alpha2beta2, the MEDH heterotetramer is composed of two large subunits and two small subunits
-
monomer
1 * 18000, cytochrome cL, SDS-PAGE
monomer
-
1 * 18000, cytochrome cL, SDS-PAGE
-
monomer
-
in contrast to other two-subunit pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenases, wide-spread in Burkholderiales, the enzyme from Methyloversatilis universalis strain FAM5 is a monosubunit protein
monomer
-
in contrast to other two-subunit pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenases, wide-spread in Burkholderiales, the enzyme from Methyloversatilis universalis strain FAM5 is a monosubunit protein
-
pentamer
2 * 65980, subunit alpha, + 2 * 7580, subunit beta, + 1 * 27860, MxaJ protein, type II MDH consists of two identical dimers of alpha and beta subunits organized to form the alpha2beta2 tetramer, and contains an additional MxaJ protein
pentamer
-
2 * 65980, subunit alpha, + 2 * 7580, subunit beta, + 1 * 27860, MxaJ protein, type II MDH consists of two identical dimers of alpha and beta subunits organized to form the alpha2beta2 tetramer, and contains an additional MxaJ protein
-
tetramer
-
2 * 65000, alpha-subunit, + 2 * 9000, beta-subunit, SDS-PAGE
tetramer
-
alpha2beta2 structure, subunit organization and structure, docking model, overview
tetramer
-
2 * 65000 + 2 * 9000
tetramer
-
alpha2beta2 structure, subunit organization and structure, docking model, overview
-
tetramer
-
2 * 65000 + 2 * 9000
-
tetramer
-
2 * 65000, alpha-subunit, + 2 * 9000, beta-subunit, SDS-PAGE
-
tetramer
2 * 65980, subunit alpha, + 2 * 7580, subunit beta, type I MDH consists of two identical dimers of alpha and beta subunits organized to form the alpha2beta2 tetramer
tetramer
alpha2beta2 MDH (MDHI)
tetramer
-
alpha2beta2 MDH (MDHI)
-
tetramer
-
2 * 65980, subunit alpha, + 2 * 7580, subunit beta, type I MDH consists of two identical dimers of alpha and beta subunits organized to form the alpha2beta2 tetramer
-
tetramer
-
2 * 62000, alpha-subunit, + 2 * 8000, beta-subunit, alpha2beta2-structure, crystal structure determination
tetramer
-
2 * 62000, alpha-subunit, + 2 * 8000, beta-subunit, alpha2beta2-structure, crystal structure determination
-
tetramer
-
heterotetramer, structure analysis and modelling, overview
tetramer
-
heterotetramer, structure analysis and modelling, overview
-
tetramer
-
alpha2beta2 subunit conposition, structure model of an alphabeta unit from crystal structure determination, overview
tetramer
2 * 66000 + 2 * 8500, alpha2beta2, crystal structure determination
tetramer
4 * 66000, alpha2beta2, crystal structure
tetramer
alpha2beta2, comparison of wild-type and mutant enzyme structures, overview
tetramer
alpha2beta2, the alpha-subunit has an 8fold radial symmetry, with its eight 3-sheets stabilized by a novel tryptophan docking motif. The PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond, subunit structures and interactions, overview
tetramer
alpha2beta2, three-dimensional structure, modelling, overview
tetramer
-
alpha2beta2, comparison of wild-type and mutant enzyme structures, overview
-
additional information
Diplococcus sp.
-
the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5
additional information
-
in contrast to other two-subunit pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenases, wide-spread in Burkholderiales, the enzyme from Methylibium petroleiphilum strain PM1 is a monosubunit protein
additional information
the alpha-subunit is known to function as the active site for the oxidoreduction reaction, which includes the PQQ group as a redox cofactor and a calcium ion coordinated to vicinal charged and hydrophobic amino-acid residues
additional information
the original conformation of the MDH Methylophaga aminisulfidivorans MPT is most likely the alpha2beta2-MxaJ complex
additional information
the original conformation of the MDH Methylophaga aminisulfidivorans MPT is most likely the alpha2beta2-MxaJ complex
additional information
-
the original conformation of the MDH Methylophaga aminisulfidivorans MPT is most likely the alpha2beta2-MxaJ complex
additional information
the MxaJ molecule consists of nine alpha-helices (alpha1-alpha9) and six beta-strands (beta1-beta6), which are partitioned to form two globular domains (domain-1 and 2). The two domains are connected by a long and rigid beta-strand (beta3) at the center, and each domain has a different arrangement of alpha/beta secondary structural element. Detailed MxaJ structure analysis, overview
additional information
the overall interaction between beta-subunits and alpha-subunits of Ma-MDH is stronger than that of terrestrial homologues, providing the structural integrity to Ma-MDH in aquatic environments
additional information
-
the MxaJ molecule consists of nine alpha-helices (alpha1-alpha9) and six beta-strands (beta1-beta6), which are partitioned to form two globular domains (domain-1 and 2). The two domains are connected by a long and rigid beta-strand (beta3) at the center, and each domain has a different arrangement of alpha/beta secondary structural element. Detailed MxaJ structure analysis, overview
-
additional information
-
the overall interaction between beta-subunits and alpha-subunits of Ma-MDH is stronger than that of terrestrial homologues, providing the structural integrity to Ma-MDH in aquatic environments
-
additional information
-
the original conformation of the MDH Methylophaga aminisulfidivorans MPT is most likely the alpha2beta2-MxaJ complex
-
additional information
-
the alpha-subunit is known to function as the active site for the oxidoreduction reaction, which includes the PQQ group as a redox cofactor and a calcium ion coordinated to vicinal charged and hydrophobic amino-acid residues
-
additional information
-
the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5
additional information
three-dimensional structrue determination of MEDH with bound methanol or ethanol, overview
additional information
-
the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5
-
additional information
-
three-dimensional structrue determination of MEDH with bound methanol or ethanol, overview
-
additional information
the large alpha-subunit has a propeller fold making up a superbarrel of eight radially arranged beta-sheets, i.e. the propeller blades, containing the tryptophan-docking motifs that link together the eight beta-sheets, and the presence in the active site of a unique eight-membered disulfide ring structure formed from adjacent cysteine residues 103 and 104, joined by an atypical non-planar peptide bond
additional information
-
the periplasmic protein contains both a PQQ-containing domain, folded into a beta-propeller fold, and a smaller cytochrome c domain, which is analogous to a typical class I c-type cytochrome, these two domains are connected via a proline-rich linker region, which lacks any secondary structure, structure model of the electron-transfer complex formed by MDH and cytochrome cL, overview
additional information
-
the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5
additional information
-
the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5
additional information
-
the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5
additional information
-
the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5
additional information
-
the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Nojiri, M.; Hira, D.; Yamaguchi, K.; Okajima, T.; Tanizawa, K.; Suzuki, S.
Crystal structures of cytochrome c(L) and methanol dehydrogenase from Hyphomicrobium denitrificans: structural and mechanistic insights into interactions between the two proteins
Biochemistry
45
3481-3492
2006
Hyphomicrobium denitrificans, Hyphomicrobium denitrificans A3151
brenda
Liu, Q.; Kirchhoff, J.R.; Faehnle, C.R.; Viola, R.E.; Hudson, R.A.
A rapid method for the purification of methanol dehydrogenase from Methylobacterium extorquens
Protein Expr. Purif.
46
316-320
2006
Methylorubrum extorquens (P16027 and P14775), Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1 (P16027 and P14775)
brenda
Williams, P.A.; Coates, L.; Mohammed, F.; Gill, R.; Erskine, P.T.; Coker, A.; Wood, S.P.; Anthony, C.; Cooper, J.B.
The atomic resolution structure of methanol dehydrogenase from Methylobacterium extorquens
Acta Crystallogr. Sect. D
D61
75-79
2005
Methylorubrum extorquens
brenda
Leopoldini, M.; Russo, N.; Toscano, M.
The preferred reaction path for the oxidation of methanol by PQQ-containing methanol dehydrogenase: addition-elimination versus hydride-transfer mechanism
Chem. Eur. J.
13
2109-2117
2007
Methylophilus methylotrophus, Methylophilus methylotrophus W3A1
brenda
Nojiri, M.; Hira, D.; Yamaguchi, K.; Okajima, T.; Tanizawa, K.; Suzuki, S.
Preparation and characterization of Ca2+-free methanol dehydrogenase from Hyphomicrobium denitrificans A3151
Chem. Lett.
34
1036-1037
2005
Hyphomicrobium denitrificans, Hyphomicrobium denitrificans A3151
-
brenda
Zhang, X.; Reddy, S.Y.; Bruice, T.C.
Mechanism of methanol oxidation by quinoprotein methanol dehydrogenase
Proc. Natl. Acad. Sci. USA
104
745-749
2007
Methylophilus methylotrophus (P38539 and P38540)
brenda
Anthony, C.
The quinoprotein dehydrogenases for methanol and glucose
Arch. Biochem. Biophys.
428
2-9
2004
Methylophilus sp., Methylorubrum extorquens (P16027 and P14775)
brenda
Richardson, I.W.; Anthony, C.
Characterization of mutant forms of the quinoprotein methanol dehydrogenase lacking an essential calcium ion
Biochem. J.
287
709-715
1992
Methylorubrum extorquens (P16027 and P14775), Methylorubrum extorquens NCIMB 9133 (P16027 and P14775)
brenda
Avezoux, A.; Goodwin, M.G.; Anthony, C.
The role of the novel disulphide ring in the active site of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens
Biochem. J.
307
735-741
1995
Methylorubrum extorquens (P16027 and P14775), Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1 (P16027 and P14775)
brenda
Goodwin, M.G.; Avezoux, A.; Dales, S.L.; Anthony, C.
Reconstitution of the quinoprotein methanol dehydrogenase from inactive Ca(2+)-free enzyme with Ca2+, Sr2+ or Ba2+
Biochem. J.
319
839-842
1996
Methylorubrum extorquens (P16027 and P14775)
brenda
White, S.; Boyd, G.; Mathews, F.S.; Xia, Z.X.; Dai, W.W.; Zhang, Y.F.; Davidson, V.L.
The active site structure of the calcium-containing quinoprotein methanol dehydrogenase
Biochemistry
32
12955-12958
1993
Methylophilus sp., Methylophilus sp. W3A1
brenda
Anthony, C.; Williams, P.
The structure and mechanism of methanol dehydrogenase
Biochim. Biophys. Acta
1647
18-23
2003
Methylophilus sp., Methylorubrum extorquens (P16027 and P14775)
brenda
Wang, X.; Sahr, F.; Xue, T.; Sun, B.
Methylobacterium salsuginis sp. nov., isolated from seawater
Int. J. Syst. Evol. Microbiol.
57
1699-1703
2007
Methylorubrum rhodesianum, Methylorubrum salsuginis, Methylobacterium oryzae, Methylobacterium oryzae MP1, Methylorubrum rhodesianum MP2
brenda
Kalyuzhnaya, M.G.; Hristova, K.R.; Lidstrom, M.E.; Chistoserdova, L.
Characterization of a novel methanol dehydrogenase in representatives of Burkholderiales: implications for environmental detection of methylotrophy and evidence for convergent evolution
J. Bacteriol.
190
3817-3823
2008
Methyloversatilis universalis, Methylibium petroleiphilum, Methyloversatilis universalis FAM5
brenda
Grosse, S.; Voigt, C.; Wendlandt, K.D.; Kleber, H.P.
Purification and properties of methanol dehydrogenase from Methylosinus sp. WI 14
J. Basic Microbiol.
38
189-196
1998
Methylosinus sp., Methylosinus sp. WI 14
brenda
Xia, Z.X.; Dai, W.W.; Xiong, J.P.; Hao, Z.P.; Davidson, V.L.; White, S.; Mathews, F.S.
The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.6-A resolution
J. Biol. Chem.
267
22289-22297
1992
Methylophilus methylotrophus (P38539 and P38540), Methylophilus methylotrophus W3A1 (P38539 and P38540)
brenda
Jongejan, A.; Jongejan, J.A.; Hagen, W.R.
Direct hydride transfer in the reaction mechanism of quinoprotein alcohol dehydrogenases: a quantum mechanical investigation
J. Comput. Chem.
22
1732-1749
2001
Methylorubrum extorquens (P16027 and P14775), Methylophilus methylotrophus (P38539 and P38540)
brenda
Williams, P.; Coates, L.; Mohammed, F.; Gill, R.; Erskine, P.; Bourgeois, D.; Wood, S.P.; Anthony, C.; Cooper, J.B.
The 1.6A X-ray structure of the unusual c-type cytochrome, cytochrome cL, from the methylotrophic bacterium Methylobacterium extorquens
J. Mol. Biol.
357
151-162
2006
Methylorubrum extorquens (P16027 and P14775)
brenda
Blake, C.C.; Ghosh, M.; Harlos, K.; Avezoux, A.; Anthony, C.
The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues
Nat. Struct. Biol.
1
102-105
1994
Methylorubrum extorquens (P16027 and P14775)
brenda
Zheng, Y.J.; Bruice, T.C.
Conformation of coenzyme pyrroloquinoline quinone and role of Ca2+ in the catalytic mechanism of quinoprotein methanol dehydrogenase
Proc. Natl. Acad. Sci. USA
94
11881-11886
1997
Methylophilus methylotrophus (P38539 and P38540), Methylophilus methylotrophus W3A1 (P38539 and P38540)
brenda
Zheng, Y.J.; Xia Zx, Y.J.; Chen Zw, Y.J.; Mathews, F.S.; Bruice, T.C.
Catalytic mechanism of quinoprotein methanol dehydrogenase: A theoretical and x-ray crystallographic investigation
Proc. Natl. Acad. Sci. USA
98
432-434
2001
Methylophilus methylotrophus (P38539 and P38540), Methylophilus methylotrophus W3A1 (P38539 and P38540)
brenda
Ghosh, M.; Anthony, C.; Harlos, K.; Goodwin, M.G.; Blake, C.
The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A
Structure
3
177-187
1995
Methylorubrum extorquens (P16027 and P14775)
brenda
Cozier, G.E.; Giles, I.G.; Anthony, C.
The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens
Biochem. J.
308
375-379
1995
Methylorubrum extorquens (P16027 and P14775)
brenda
Suzuki, R.; Lisdiyanti, P.; Komagata, K.; Uchimura, T.
MxaF gene, a gene encoding alpha subunit of methanol dehydrogenase in and false growth of acetic acid bacteria on methanol
J. Gen. Appl. Microbiol.
55
101-110
2009
Acidomonas methanolica, no activity in Acetobacter malorum, no activity in Acetobacter pomorum, no activity in Acetobacter lovaniensis, no activity in Acetobacter malorum DSM 14337T, no activity in Acetobacter pomorum DSM 11825T
brenda
Idupulapati, N.B.; Mainardi, D.S.
Quantum chemical modeling of methanol oxidation mechanisms by methanol dehydrogenase enzyme: effect of substitution of calcium by barium in the active site
J. Phys. Chem. A
114
1887-1896
2010
Methylorubrum extorquens
brenda
Choi, J.M.; Kim, H.G.; Kim, J.S.; Youn, H.S.; Eom, S.H.; Yu, S.L.; Kim, S.W.; Lee, S.H.
Purification, crystallization and preliminary X-ray crystallographic analysis of a methanol dehydrogenase from the marine bacterium Methylophaga aminisulfidivorans MP(T)
Acta Crystallogr. Sect. F
67
513-516
2011
Methylophaga aminisulfidivorans (A3FJ51), Methylophaga aminisulfidivorans MPT (A3FJ51)
brenda
Li, J.; Gan, J.H.; Mathews, F.S.; Xia, Z.X.
The enzymatic reaction-induced configuration change of the prosthetic group PQQ of methanol dehydrogenase
Biochem. Biophys. Res. Commun.
406
621-626
2011
Methylophilus methylotrophus (P38539), Methylophilus methylotrophus W3A1 (P38539)
brenda
Gvozdev, A.; Tukhvatullin, I.; Gvozdev, R.
Quinone-dependent alcohol dehydrogenases and FAD-dependent alcohol oxidases
Biochemistry
77
843-856
2012
Methylorubrum extorquens, Methylophilus methylotrophus, Paracoccus denitrificans, Paracoccus pantotrophus, Pseudomonas sp., Rhodoblastus acidophilus, Diplococcus sp., Methylophilus methylotrophus W3A1
brenda
Kim, H.G.; Han, G.H.; Kim, D.; Choi, J.S.; Kim, S.W.
Comparative analysis of two types of methanol dehydrogenase from Methylophaga aminisulfidivorans MPT grown on methanol
J. Basic Microbiol.
52
141-149
2012
Methylophaga aminisulfidivorans (A3FJ49), Methylophaga aminisulfidivorans (A3FJ51), Methylophaga aminisulfidivorans, Methylophaga aminisulfidivorans MPT (A3FJ49), Methylophaga aminisulfidivorans MPT (A3FJ51)
brenda
Kim, H.G.; Kim, S.W.
Purification and characterization of a methanol dehydrogenase derived from Methylomicrobium sp. HG-1 cultivated using a compulsory circulation diffusion system
Biotechnol. Bioprocess Eng.
11
134-139
2006
Methylomicrobium sp. HG-1
-
brenda
Ghosh, S.; Dhanasingh, I.; Ryu, J.; Kim, S.W.; Lee, S.H.
Crystal structure of cytochrome cL from the aquatic methylotrophic bacterium Methylophaga aminisulfidivorans MP
J. Microbiol. Biotechnol.
30
1261-1271
2020
Methylophaga aminisulfidivorans (A3FJ48 AND A3FJ51 AND A3FJ49), Methylophaga aminisulfidivorans MP (A3FJ48 AND A3FJ51 AND A3FJ49)
brenda
Myung Choi, J.; Cao, T.P.; Wouk Kim, S.; Ho Lee, K.; Haeng Lee, S.
MxaJ structure reveals a periplasmic binding protein-like architecture with unique secondary structural elements
Proteins
85
1379-1386
2017
Methylophaga aminisulfidivorans (A3FJ48 AND A3FJ51 AND A3FJ49), Methylophaga aminisulfidivorans MP (A3FJ48 AND A3FJ51 AND A3FJ49)
brenda