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.

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

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
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
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.