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Literature summary extracted from

  • Gvozdev, A.; Tukhvatullin, I.; Gvozdev, R.
    Quinone-dependent alcohol dehydrogenases and FAD-dependent alcohol oxidases (2012), Biochemistry, 77, 843-856.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.2.7 membrane
-
 Paracoccus denitrificans 16020
-
1.1.2.7 membrane
-
 Pseudomonas sp. 16020
-
1.1.2.7 membrane
-
 Methylophilus methylotrophus 16020
-
1.1.2.7 membrane
-
 Methylorubrum extorquens 16020
-
1.1.2.7 membrane
-
 Paracoccus pantotrophus 16020
-
1.1.2.7 membrane
-
 Rhodoblastus acidophilus 16020
-
1.1.2.7 membrane
-
 Diplococcus sp. 16020
-
1.1.2.7 soluble
-
 Paracoccus denitrificans
-
-
1.1.2.7 soluble
-
 Pseudomonas sp.
-
-
1.1.2.7 soluble
-
 Methylophilus methylotrophus
-
-
1.1.2.7 soluble
-
 Methylorubrum extorquens
-
-
1.1.2.7 soluble
-
 Paracoccus pantotrophus
-
-
1.1.2.7 soluble
-
 Rhodoblastus acidophilus
-
-
1.1.2.7 soluble
-
 Diplococcus sp.
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.2.7 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 Paracoccus denitrificans
1.1.2.7 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 Pseudomonas sp.
1.1.2.7 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 Methylophilus methylotrophus
1.1.2.7 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 Methylorubrum extorquens
1.1.2.7 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 Paracoccus pantotrophus
1.1.2.7 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 Rhodoblastus acidophilus
1.1.2.7 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 Diplococcus sp.
1.1.5.5 Ca2+ required, two ions, one bound in the active site, and one away from the active site near the N-terminus of the molecule. Dimensions of the active site cavity are provided by the stabilization of the spatial enzyme structure by the second Ca2+ ion Pseudomonas sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.2.7 methanol + 2 ferricytochrome cL Pseudomonas sp. cytochrome c is the natural electron acceptor formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL Methylophilus methylotrophus cytochrome c is the natural electron acceptor formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL Methylorubrum extorquens cytochrome c is the natural electron acceptor formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL Paracoccus pantotrophus cytochrome c is the natural electron acceptor formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL Rhodoblastus acidophilus cytochrome c is the natural electron acceptor formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL Diplococcus sp. cytochrome c is the natural electron acceptor formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL Paracoccus denitrificans 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 formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL Methylophilus methylotrophus W3A1 cytochrome c is the natural electron acceptor formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.5.5 ethanol + ubiquinone Pseudomonas sp.
-
 acetaldehyde + ubiquinol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.2.7 Diplococcus sp.
-
-
-
1.1.2.7 Methylophilus methylotrophus
-
-
-
1.1.2.7 Methylophilus methylotrophus W3A1
-
-
-
1.1.2.7 Methylorubrum extorquens
-
-
-
1.1.2.7 Paracoccus denitrificans
-
-
-
1.1.2.7 Paracoccus pantotrophus
-
-
-
1.1.2.7 Pseudomonas sp.
-
-
-
1.1.2.7 Rhodoblastus acidophilus
-
-
-
1.1.5.5 Pseudomonas sp.
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.2.7 a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+ mechanism of methanol oxidation by QMDH, overview Paracoccus denitrificans
a
1.1.2.7 a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+ mechanism of methanol oxidation by QMDH, overview Pseudomonas sp.
a
1.1.2.7 a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+ mechanism of methanol oxidation by QMDH, overview Methylophilus methylotrophus
a
1.1.2.7 a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+ mechanism of methanol oxidation by QMDH, overview Methylorubrum extorquens
a
1.1.2.7 a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+ mechanism of methanol oxidation by QMDH, overview Paracoccus pantotrophus
a
1.1.2.7 a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+ mechanism of methanol oxidation by QMDH, overview Rhodoblastus acidophilus
a
1.1.2.7 a primary alcohol + 2 ferricytochrome cL = an aldehyde + 2 ferrocytochrome cL + 2 H+ mechanism of methanol oxidation by QMDH, overview Diplococcus sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.2.7 methanol + 2 ferricytochrome cL
-
 Paracoccus denitrificans formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL
-
 Pseudomonas sp. formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL
-
 Methylophilus methylotrophus formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL
-
 Methylorubrum extorquens formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL
-
 Paracoccus pantotrophus formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL
-
 Rhodoblastus acidophilus formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL
-
 Diplococcus sp. formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL cytochrome c is the natural electron acceptor Pseudomonas sp. formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL cytochrome c is the natural electron acceptor Methylophilus methylotrophus formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL cytochrome c is the natural electron acceptor Methylorubrum extorquens formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL cytochrome c is the natural electron acceptor Paracoccus pantotrophus formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL cytochrome c is the natural electron acceptor Rhodoblastus acidophilus formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL cytochrome c is the natural electron acceptor Diplococcus sp. formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL 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 Paracoccus denitrificans formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL
-
 Methylophilus methylotrophus W3A1 formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 methanol + 2 ferricytochrome cL cytochrome c is the natural electron acceptor Methylophilus methylotrophus W3A1 formaldehyde + 2 ferrocytochrome cL + 2 H+
-
 ?
1.1.2.7 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 Paracoccus denitrificans ?
-
 ?
1.1.2.7 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 Pseudomonas sp. ?
-
 ?
1.1.2.7 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 Methylophilus methylotrophus ?
-
 ?
1.1.2.7 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 Methylorubrum extorquens ?
-
 ?
1.1.2.7 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 Paracoccus pantotrophus ?
-
 ?
1.1.2.7 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 Rhodoblastus acidophilus ?
-
 ?
1.1.2.7 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 Diplococcus sp. ?
-
 ?
1.1.2.7 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 Methylophilus methylotrophus W3A1 ?
-
 ?
1.1.5.5 ethanol + ubiquinone
-
 Pseudomonas sp. acetaldehyde + ubiquinol
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.2.7 More 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 Paracoccus denitrificans
1.1.2.7 More 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 Pseudomonas sp.
1.1.2.7 More 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 Methylophilus methylotrophus
1.1.2.7 More 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 Methylorubrum extorquens
1.1.2.7 More 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 Paracoccus pantotrophus
1.1.2.7 More 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 Rhodoblastus acidophilus
1.1.2.7 More 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 Diplococcus sp.
1.1.5.5 homodimer two alpha-subunits Pseudomonas sp.
1.1.5.5 More the enzyme shows a propeller structure, QEDH contains a disulfide structure that is similar to the analogous structure in QMDH, EC 1.1.2.8 Pseudomonas sp.

Synonyms

EC Number Synonyms Comment Organism
1.1.2.7 PQQ-dependent methanol dehydrogenase
-
 Paracoccus denitrificans
1.1.2.7 PQQ-dependent methanol dehydrogenase
-
 Pseudomonas sp.
1.1.2.7 PQQ-dependent methanol dehydrogenase
-
 Methylophilus methylotrophus
1.1.2.7 PQQ-dependent methanol dehydrogenase
-
 Methylorubrum extorquens
1.1.2.7 PQQ-dependent methanol dehydrogenase
-
 Paracoccus pantotrophus
1.1.2.7 PQQ-dependent methanol dehydrogenase
-
 Rhodoblastus acidophilus
1.1.2.7 PQQ-dependent methanol dehydrogenase
-
 Diplococcus sp.
1.1.2.7 QMDH
-
 Paracoccus denitrificans
1.1.2.7 QMDH
-
 Pseudomonas sp.
1.1.2.7 QMDH
-
 Methylophilus methylotrophus
1.1.2.7 QMDH
-
 Methylorubrum extorquens
1.1.2.7 QMDH
-
 Paracoccus pantotrophus
1.1.2.7 QMDH
-
 Rhodoblastus acidophilus
1.1.2.7 QMDH
-
 Diplococcus sp.
1.1.2.7 quinone-dependent alcohol dehydrogenase
-
 Paracoccus denitrificans
1.1.2.7 quinone-dependent alcohol dehydrogenase
-
 Pseudomonas sp.
1.1.2.7 quinone-dependent alcohol dehydrogenase
-
 Methylophilus methylotrophus
1.1.2.7 quinone-dependent alcohol dehydrogenase
-
 Methylorubrum extorquens
1.1.2.7 quinone-dependent alcohol dehydrogenase
-
 Paracoccus pantotrophus
1.1.2.7 quinone-dependent alcohol dehydrogenase
-
 Rhodoblastus acidophilus
1.1.2.7 quinone-dependent alcohol dehydrogenase
-
 Diplococcus sp.
1.1.2.7 quinoprotein methanol dehydrogenase
-
 Paracoccus denitrificans
1.1.2.7 quinoprotein methanol dehydrogenase
-
 Pseudomonas sp.
1.1.2.7 quinoprotein methanol dehydrogenase
-
 Methylophilus methylotrophus
1.1.2.7 quinoprotein methanol dehydrogenase
-
 Methylorubrum extorquens
1.1.2.7 quinoprotein methanol dehydrogenase
-
 Paracoccus pantotrophus
1.1.2.7 quinoprotein methanol dehydrogenase
-
 Rhodoblastus acidophilus
1.1.2.7 quinoprotein methanol dehydrogenase
-
 Diplococcus sp.
1.1.5.5 PQQ-dependent ethanol dehydrogenase
-
 Pseudomonas sp.
1.1.5.5 quinone-dependent alcohol dehydrogenase
-
 Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.2.7 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 Paracoccus denitrificans
1.1.2.7 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 Pseudomonas sp.
1.1.2.7 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 Methylophilus methylotrophus
1.1.2.7 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 Methylorubrum extorquens
1.1.2.7 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 Paracoccus pantotrophus
1.1.2.7 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 Rhodoblastus acidophilus
1.1.2.7 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 Diplococcus sp.
1.1.5.5 pyrroloquinoline quinone i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid Pseudomonas sp.