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Literature summary for 1.1.2.7 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

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

Metals/Ions

Metals/Ions Comment Organism Structure
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
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.
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
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
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
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
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.

Natural Substrates/ Products (Substrates)

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

Organism

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

Reaction

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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
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.
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
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
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
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
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.

Synonyms

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

Cofactor

Cofactor Comment Organism 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 Paracoccus denitrificans
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.
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
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
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
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
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.