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Enzyme Nomenclature
Information on EC 1.1.2.8 - alcohol dehydrogenase (cytochrome c)
for references in articles please use BRENDA:EC1.1.2.8
Word Map on EC 1.1.2.8
- 1.1.2.8
- aldehyde
-
pichia
-
pastoris
-
quinone-dependent
-
quinoprotein
- pqq-adh
- environmental protection
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.1.2.8
-
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RECOMMENDED NAME
GeneOntology No.
alcohol dehydrogenase (cytochrome c)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a primary alcohol + 2 ferricytochrome c = an aldehyde + 2 ferrocytochrome c + 2 H+
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
alcohol:cytochrome c oxidoreductase
A periplasmic PQQ-containing quinoprotein. Occurs in Pseudomonas and Rhodopseudomonas. The enzyme from Pseudomonas aeruginosa uses a specific inducible cytochrome c550 as electron acceptor. Acts on a wide range of primary and secondary alcohols, but not methanol. It has a homodimeric structure [contrasting with the heterotetrameric structure of EC 1.1.2.7, methanol dehydrogenase (cytochrome c)]. It is routinely assayed with phenazine methosulfate as electron acceptor. Activity is stimulated by ammonia or amines. Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene adhA encoding subunit I; isolated from passion fruit
UniProt
gene adhB encoding subunit II; isolated from passion fruit
UniProt
gene adhS encoding the smallest subunit, subunit III, genes adhA and adhB encode subunits I and II
-
-
gene adhA encoding subunit I; isolated from passion fruit
UniProt
gene adhB encoding subunit II; isolated from passion fruit
UniProt
gene adhS encoding the smallest subunit, subunit III, genes adhA and adhB encode subunits I and II
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
evolution
-
quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
evolution
-
quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
evolution
-
ADHs are categorized into three groups (type I, II, and III ADHs) according to their domain structure and localization. Type I ADHs have molecular and enzymatic properties that are very similar to those of methanol dehydrogenases, MDHs, but they have a low affinity for methanol. Type I ADHs, on the other hand, generally use ethylamine or methylamine as essential activators instead of ammonia
evolution
-
quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
-
evolution
-
ADHs are categorized into three groups (type I, II, and III ADHs) according to their domain structure and localization. Type I ADHs have molecular and enzymatic properties that are very similar to those of methanol dehydrogenases, MDHs, but they have a low affinity for methanol. Type I ADHs, on the other hand, generally use ethylamine or methylamine as essential activators instead of ammonia
-
evolution
-
quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
-
evolution
-
quinoprotein alcohol dehydrogenase usually occupies PQQ as a cofactor and belongs to the family of PQQ-dependent type I alcohol dehydrogenases, sequence comparisons and phylogenetic tree
-
malfunction
-
an exaF mutant is not affected for growth with ethanol
malfunction
single deletions of genes coding for PQQ-dependent alcohol dehydrogenases PedE and PedH have only minor effects on growth rates, indicating that Pseudomonas putida strain KT2440 can use both enzymes in a redundant fashion for the metabolization of butanol. Growth of mutants lacking PedE and PedH on n-butanol is significantly impaired, but not completely inhibited, suggesting that additional alcohol dehydrogenases can at least partially complement their function in strain KT2440; single deletions of genes coding for PQQ-dependent alcohol dehydrogenases PedE and PedH have only minor effects on growth rates, indicating that Pseudomonas putida strain KT2440 can use both enzymes in a redundant fashion for the metabolization of butanol. Growth of mutants lacking PedE and PedH on n-butanol is significantly impaired, but not completely inhibited, suggesting that additional alcohol dehydrogenases can at least partially complement their function in strain KT2440
malfunction
Methylobacterium extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
an exaF mutant is not affected for growth with ethanol
-
malfunction
-
single deletions of genes coding for PQQ-dependent alcohol dehydrogenases PedE and PedH have only minor effects on growth rates, indicating that Pseudomonas putida strain KT2440 can use both enzymes in a redundant fashion for the metabolization of butanol. Growth of mutants lacking PedE and PedH on n-butanol is significantly impaired, but not completely inhibited, suggesting that additional alcohol dehydrogenases can at least partially complement their function in strain KT2440; single deletions of genes coding for PQQ-dependent alcohol dehydrogenases PedE and PedH have only minor effects on growth rates, indicating that Pseudomonas putida strain KT2440 can use both enzymes in a redundant fashion for the metabolization of butanol. Growth of mutants lacking PedE and PedH on n-butanol is significantly impaired, but not completely inhibited, suggesting that additional alcohol dehydrogenases can at least partially complement their function in strain KT2440
-
metabolism
butanol is oxidized to butyraldehyde by PedE and PedH and then further oxidized to butyric acid by the aldehyde dehydrogenase PedI. Both enzymes, PedE and PedH, are directly involved in butanol oxidation in Pseudomonas putida KT2440; butanol is oxidized to butyraldehyde by PedE and PedH and then further oxidized to butyric acid by the aldehyde dehydrogenase PedI. Both enzymes, PedE and PedH, are directly involved in butanol oxidation in Pseudomonas putida KT2440
metabolism
-
butanol is oxidized to butyraldehyde by PedE and PedH and then further oxidized to butyric acid by the aldehyde dehydrogenase PedI. Both enzymes, PedE and PedH, are directly involved in butanol oxidation in Pseudomonas putida KT2440; butanol is oxidized to butyraldehyde by PedE and PedH and then further oxidized to butyric acid by the aldehyde dehydrogenase PedI. Both enzymes, PedE and PedH, are directly involved in butanol oxidation in Pseudomonas putida KT2440
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physiological function
the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation; the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation; the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation; the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation; the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation; the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation; the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation; the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation
physiological function
-
the enzyme is involved in diethylstilbestrol degradation
physiological function
-
the enzyme is involved in diethylstilbestrol degradation
physiological function
-
the enzyme is involved in diethylstilbestrol degradation
physiological function
-
ExaF contributes to ethanol metabolism when La3 is present, expanding the role of lanthanides to multicarbon metabolism. ExaA quinoprotein ethanol dehydrogenase, and not the type I ADH,EC 1.1.2.4, is responsible for methanol oxidation in the MDH-3 mutant strain
physiological function
-
the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation; the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation; the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation
-
physiological function
-
the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation; the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation
-
physiological function
-
the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation; the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation; the ADH involved in ethanol oxidation of the thermotolerant strain is important for the high temperature fermentation
-
physiological function
Methylobacterium extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
ExaF contributes to ethanol metabolism when La3 is present, expanding the role of lanthanides to multicarbon metabolism. ExaA quinoprotein ethanol dehydrogenase, and not the type I ADH,EC 1.1.2.4, is responsible for methanol oxidation in the MDH-3 mutant strain
-
physiological function
-
the enzyme is involved in diethylstilbestrol degradation
-
physiological function
-
the enzyme is involved in diethylstilbestrol degradation
-
physiological function
-
the enzyme is involved in diethylstilbestrol degradation
-
additional information
-
the enzyme occurs in active and inactive forms, overview. Active ADHa is brought back by ethanol to its full reduction state, but in inactive ADHi, only one-quarter of the total heme c is reduced, pH dependencies and redox potentials of cofactors, overview
additional information
-
Thr104 might be involved in molecular coupling with subunit I in order to construct active ADH complex, whereas 22 amino acid residues at C-terminal may be not necessary for PQQ-ADH activity
additional information
-
ExaF homology modeling using the crystal structure of the quinoprotein ethanol dehydrogenase QEDH from Pseudomonas aeruginosa, PDB 1FLG, overview. Residues E198, D317, D319, and N275 form the active site. Residue D319 might be necessary for lanthanide coordination next to catalytic aspartate D317
additional information
-
Thr104 might be involved in molecular coupling with subunit I in order to construct active ADH complex, whereas 22 amino acid residues at C-terminal may be not necessary for PQQ-ADH activity
-
additional information
-
the enzyme occurs in active and inactive forms, overview. Active ADHa is brought back by ethanol to its full reduction state, but in inactive ADHi, only one-quarter of the total heme c is reduced, pH dependencies and redox potentials of cofactors, overview
-
additional information
Methylobacterium extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
ExaF homology modeling using the crystal structure of the quinoprotein ethanol dehydrogenase QEDH from Pseudomonas aeruginosa, PDB 1FLG, overview. Residues E198, D317, D319, and N275 form the active site. Residue D319 might be necessary for lanthanide coordination next to catalytic aspartate D317
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
ethanol + N,N,N',N'-tetramethyl-p-phenylenediamine
ethanal + ?
-
i.e. Wurster's Blue
-
-
?
ethanol + oxidized 2,6-dichlorophenolindophenol
ethanal + reduced 2,6-dichlorophenolindophenol
butanol + 2 cytochrome c
butyraldehyde + 2 reduced cytochrome c
-
-
-
r
butanol + 2 cytochrome c
butyraldehyde + 2 reduced cytochrome c
-
-
-
r
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
-
-
-
-
r
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
Methylobacterium extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
-
-
-
r
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
-
-
-
r
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
-
-
-
r
ethanol + 2 cytochrome c
ethanal + 2 reduced cytochrome c
-
EPR-study to elucidate reaction mechanism. In an addition/elimination mechanism, the negatively charged substrate oxygen then performs a nucleophilic addition to the PQQ(C5) to form a covalent substrate-PQQ complex. This is followed by elimination of ethanal, leaving the fully reduced PQQH2. In a hydride transfer mechanism, a nucleophilic addition to the PQQ(C5) again occurs, but this time it is the hydride from C1 of the substrate that is transferred, completing the oxidization of the ethanol to ethanal. Subsequently, the PQQ enolizes to form PQQH2. The results are consistent with either proposed mechanism
-
-
-
ethanol + 2 cytochrome c
ethanal + 2 reduced cytochrome c
-
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
?
ethanol + oxidized 2,6-dichlorophenolindophenol
ethanal + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
ethanol + oxidized 2,6-dichlorophenolindophenol
ethanal + reduced 2,6-dichlorophenolindophenol
-
-
-
?
methanol + 2 cytochrome c
formaldehyde + 2 reduced cytochrome c
-
-
-
-
r
methanol + 2 cytochrome c
formaldehyde + 2 reduced cytochrome c
-
the maximal reaction velocity of ExaF-La for formaldehyde is 23% greater than for methanol as the substrate
-
-
r
methanol + 2 cytochrome c
formaldehyde + 2 reduced cytochrome c
Methylobacterium extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
-
-
-
r
methanol + 2 cytochrome c
formaldehyde + 2 reduced cytochrome c
Methylobacterium extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
the maximal reaction velocity of ExaF-La for formaldehyde is 23% greater than for methanol as the substrate
-
-
r
propanol + 2 cytochrome c
propanal + 2 reduced cytochrome c
-
-
-
-
?
additional information
?
-
-
ExaF is functionally an ethanol dehydrogenase, with secondary activities with formaldehyde, methanol, and acetaldehyde. Enzyme assays are performed with with the artificial electron acceptors phenazine methosulfate and 2,6-dichlorophenolindophenol. Methanol-independent reduction of the latter is not observed with purified enzyme
-
-
-
additional information
?
-
Methylobacterium extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
ExaF is functionally an ethanol dehydrogenase, with secondary activities with formaldehyde, methanol, and acetaldehyde. Enzyme assays are performed with with the artificial electron acceptors phenazine methosulfate and 2,6-dichlorophenolindophenol. Methanol-independent reduction of the latter is not observed with purified enzyme
-
-
-
additional information
?
-
-
enzyme assays are performed with with the artificial electron acceptors phenazine methosulfate and 2,6-dichlorophenolindophenol
-
-
-
additional information
?
-
-
enzyme assays are performed with with the artificial electron acceptors phenazine methosulfate and 2,6-dichlorophenolindophenol
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
butanol + 2 cytochrome c
butyraldehyde + 2 reduced cytochrome c
B1N7J0, B1N7J5
-
-
-
r
butanol + 2 cytochrome c
butyraldehyde + 2 reduced cytochrome c
B1N7J0, B1N7J5
-
-
-
r
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
diethylstilbestrol + pyrroloquinoline quinone
diethylstilbestrol 4-semiquinone + pyrroloquinoline quinol
-
i.e. 4,4'-(3E)-hex-3-ene-3,4-diyldiphenol
-
-
?
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
-
-
-
-
r
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
Methylobacterium extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
-
-
-
r
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
B1N7J0, B1N7J5
-
-
-
r
ethanol + 2 cytochrome c
acetaldehyde + 2 reduced cytochrome c
B1N7J0, B1N7J5
-
-
-
r
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
C7G3B7, C7G3B8, C9K501, C9K502, C9K504, C9W9E3, D2SZY4, D2SZY5
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
C9K501, C9K502, C9K504
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
C7G3B7, C7G3B8
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
-
-
-
-
?
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
C9W9E3, D2SZY4, D2SZY5
-
-
-
?
methanol + 2 cytochrome c
formaldehyde + 2 reduced cytochrome c
-
-
-
-
r
methanol + 2 cytochrome c
formaldehyde + 2 reduced cytochrome c
Methylobacterium extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
-
-
-
r
additional information
?
-
-
ExaF is functionally an ethanol dehydrogenase, with secondary activities with formaldehyde, methanol, and acetaldehyde. Enzyme assays are performed with with the artificial electron acceptors phenazine methosulfate and 2,6-dichlorophenolindophenol. Methanol-independent reduction of the latter is not observed with purified enzyme
-
-
-
additional information
?
-
Methylobacterium extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
ExaF is functionally an ethanol dehydrogenase, with secondary activities with formaldehyde, methanol, and acetaldehyde. Enzyme assays are performed with with the artificial electron acceptors phenazine methosulfate and 2,6-dichlorophenolindophenol. Methanol-independent reduction of the latter is not observed with purified enzyme
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyrroloquinoline quinone
-
the binding pocket of pyrroloquinoline quinone contains a characteristic disulphide ring formed by two adjacent cysteine residues. Analysis by EPR spectroscopy shows that the disulfide ring is no prerequisite for the formation of the functionally important semiquinone form of pyrroloquinoline quinone
pyrroloquinoline quinone
-
i.e. 2,7,9-tricarboxy-1H-pyrrolo-[2,3-f]quinoline-4,5-dione
pyrroloquinoline quinone
PQQ, a prosthetic group; PQQ, a prosthetic group
additional information
-
enzyme assays are performed with the artificial electron acceptors phenazine methosulfate and 2,6-dichlorophenolindophenol
-
additional information
-
enzyme assays are performed with the artificial electron acceptors phenazine methosulfate and 2,6-dichlorophenolindophenol
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
La3+
-
required, active site-bound, 1.3 mol of La3+ per mol of ExaF protomer, indicating a 1:1 ratio of L3+ to protomer of enzyme
Sr2+
-
incubation of apo-enzyme with Sr2+ and pyrroloquinoline quinone leads to the formation of an active Sr2+-form. The Sr2+ and the Ca2+-forms of the enzyme differ in their absorption spectra. The Sr2+-form is inactivated by trans-l,2-diaminocyclohexane-N,N,N',N'-tetraacetic acid twice as fast as the Ca2+-form.
additional information
-
the enzyme from strain AM1 utilizes La3+ rather than Ca2+ as a cofactor
Ca2+
-
the prosthetic group is located in the centre of the superbarrel and is coordinated to a calcium ion.In addition, enzyme contains a second Ca2+-binding site at the N-terminus, which contributes to the stability of the native enzyme
Ca2+
-
contains one Ca2+ ion per subunit of native enzyme. Treatment with trans-l,2-diaminocyclohexane-N,N,N',N'-tetraacetic acid at 30°C leads to an catalytically inactive apo-form. Upon incubation of the apo-form with Ca2 + and pyrroloquinoline quinone a fully active holo-enzyme is reconstituted. Incubation of apo-enzyme with Sr2+ and pyrroloquinoline quinone leads to the formation of an active Sr2+-form. The Sr2+ and the Ca2+-forms of the enzyme differ in their absorption spectra.
Ca2+
-
rather loosely bound, necessary for pyrroloquinoline quinone binding and for stability of enzyme
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ethylamine
-
activating at low concentrations, inhibitory at high concentrations
pentylamine
-
the alcohol oxidation activity of PpADH is strongly enhanced by pentylamine and the affinity for substrates is also improved by pentylamine as an activator, inhibitory at high concentrations
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ethanol
-
does not affect the adhS gene expression but induces PQQ-ADH activity
pentylamine
-
the alcohol oxidation activity of PpADH is strongly enhanced by pentylamine and the affinity for substrates is also improved by pentylamine as an activator, inhibitory at high concentrations
additional information
-
the enzyme requires ammonia or primary amines as activators in in vitro assays with artificial electron acceptors, the enzyme is activated by various primary amines, dimethylamine, and trimethylamine. tert-Butylamine is a poor activator. The hydrophobic interaction contributes to the binding of amine activators to the binding site in the enzyme
-
methylamine
-
methylamine is a 5fold better activator for enzyme ExaF in vitro than ammonium
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
ethanol
-
pH 9.0, temperature not specified in the publication, in presence of pentylamine
0.21
ethanol
-
pH 9.0, temperature not specified in the publication, in presence of ethylamine
0.35
Propanol
-
pH 9.0, temperature not specified in the publication, in presence of pentylamine
0.43
Propanol
-
pH 9.0, temperature not specified in the publication, in presence of ethylamine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24.8
ethanol
-
pH 9.0, temperature not specified in the publication, in presence of ethylamine
56.6
ethanol
-
pH 9.0, temperature not specified in the publication, in presence of pentylamine
32.6
Propanol
-
pH 9.0, temperature not specified in the publication, in presence of ethylamine
73.1
Propanol
-
pH 9.0, temperature not specified in the publication, in presence of pentylamine
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
115
ethanol
-
pH 9.0, temperature not specified in the publication, in presence of ethylamine
395
ethanol
-
pH 9.0, temperature not specified in the publication, in presence of pentylamine
73
Propanol
-
pH 9.0, temperature not specified in the publication, in presence of ethylamine
209
Propanol
-
pH 9.0, temperature not specified in the publication, in presence of pentylamine
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
additional information
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
additional information
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
additional information
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
additional information
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
additional information
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
additional information
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
additional information
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
additional information
-
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
-
additional information
-
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
-
additional information
-
the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol; the MSU10 strain shows higher acetic acid productivity in a medium containing 6% ethanol at 37°C than strain SKU1108, while strain SKU1108 strain can accumulate more acetic acid in a medium supplemented with 4-5% ethanol at the same temperature. The fermentation ability at 37°C of these thermotolerant strains is superior to that of mesophilic strain IFO3191 having weak growth and very delayed acetic acid production at 37°C even at 4% ethanol
-
additional information
-
ADH is largely expressed in its active form
additional information
-
ADH is largely expressed in its active form
-
additional information
-
growth rate constants of Methylobacterium extorquens wild-type and mutant strains grown with ethanol as the carbon source
additional information
Methylobacterium extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
growth rate constants of Methylobacterium extorquens wild-type and mutant strains grown with ethanol as the carbon source
-
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9000
45000
-
1 * 72000 + 1 * 45000, inactive enzyme form, SDS-PAGE; 2 * 72000 + 2 * 45000, dimer of dimers, active enzyme form, SDS-PAGE
60000
72000
-
1 * 72000 + 1 * 45000, inactive enzyme form, SDS-PAGE; 2 * 72000 + 2 * 45000, dimer of dimers, active enzyme form, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
heterotetramer
homodimer
tetramer
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2 * 60000, alpha-subunit, + 2 * 9000, beta-subunit, SDS-PAGE
additional information
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enzyme interacts with a soluble cytochrome cEDH, the oxidized form being an excellent acceptor for the semiquinone form of EDH. This cytochrome is quite different from the cytochrome c551 operating in nitrate respiration
heterodimer
-
1 * 72000 + 1 * 45000, inactive enzyme form, SDS-PAGE
heterodimer
-
1 * 72000 + 1 * 45000, inactive enzyme form, SDS-PAGE
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heterotetramer
-
2 * 72000 + 2 * 45000, dimer of dimers, active enzyme form, SDS-PAGE
heterotetramer
-
2 * 72000 + 2 * 45000, dimer of dimers, active enzyme form, SDS-PAGE
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homodimer
Methylobacterium extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
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2 * 61000, recombinant His6-tagged enzyme, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
sequence contains a signal peptide of 34 residues
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alignment with the amino acid sequence of the large subunit of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens. The amino acid residues involved in the binding of pyrroloquinoline quinone and Ca2+ at the active site are conserved
to 2.6 A resolution, by molecular replacement. Eight W-shaped beta-sheet motifs are arranged circularly in a propeller-like fashion forming a disk-shaped superbarrel. The prosthetic group is located in the centre of the superbarrel and is coordinated to a calcium ion. Most amino acid residues found in close contact with the prosthetic group pyrroloquinoline quinone and the Ca2+ are conserved between the quinoprotein ethanol dehydrogenase structure and that of the methanol dehydrogenases from Methylobacterium extorquens or Methylophilus W3A1. The main differences in the active-site region are a bulky tryptophan residue in the active-site cavity of methanol dehydrogenase, which is replaced by a phenylalanine and a leucine side-chain in the ethanol dehydrogenase structure and a leucine residue right above the pyrrolquinoline quinone group in methanol dehydrogenase which is replaced by a tryptophan side-chain. Both amino acid exchanges contribute to different substrate specificities of these otherwise very similar enzymes. In addition to the Ca2+ in the active-site cavity, ethanol dehydrogenase contains a second Ca2+-binding site at the N-terminus, which contributes to the stability of the native enzyme
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetic acid
acetic acid
ADH from strain IFO3191 retains 36% of the activities after treating with 2% acetic acid at 30°C for 30 min, and 45% after incubation with 4% acetic acid at 25°C for 30 min, unstable in 4% acetic acid at 30°C; ADH from strain IFO3191 retains 36% of the activities after treating with 2% acetic acid at 30°C for 30 min, and 45% after incubation with 4% acetic acid at 25°C for 30 min, unstable in 4% acetic acid at 30°C; ADH from strain IFO3191 retains 36% of the activities after treating with 2% acetic acid at 30°C for 30 min, and 45% after incubation with 4% acetic acid at 25°C for 30 min, unstable in 4% acetic acid at 30°C; ADH from strain MSU10 shows the highest resistance to acetic acid. The enzyme retains over 90% of the original activity after 30 min incubation with 2% acetic acid at 30°C and also with 4% acetic acid at 25°C, unstable in 4% acetic acid at 30°C; ADH from strain MSU10 shows the highest resistance to acetic acid. The enzyme retains over 90% of the original activity after 30 min incubation with 2% acetic acid at 30°C and also with 4% acetic acid at 25°C, unstable in 4% acetic acid at 30°C; ADH from strain SKU1108 retains 61% of the activities after treating with 2% acetic acid at 30°C for 30 min, and 79% after incubation with 4% acetic acid at 25°C for 30 min, unstable in 4% acetic acid at 30°C; ADH from strain SKU1108 retains 61% of the activities after treating with 2% acetic acid at 30°C for 30 min, and 79% after incubation with 4% acetic acid at 25°C for 30 min, unstable in 4% acetic acid at 30°C; ADH from strain SKU1108 retains 61% of the activities after treating with 2% acetic acid at 30°C for 30 min, and 79% after incubation with 4% acetic acid at 25°C for 30 min, unstable in 4% acetic acid at 30°C
acetic acid
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ADH from strain IFO3191 retains 36% of the activities after treating with 2% acetic acid at 30°C for 30 min, and 45% after incubation with 4% acetic acid at 25°C for 30 min, unstable in 4% acetic acid at 30°C; ADH from strain IFO3191 retains 36% of the activities after treating with 2% acetic acid at 30°C for 30 min, and 45% after incubation with 4% acetic acid at 25°C for 30 min, unstable in 4% acetic acid at 30°C; ADH from strain IFO3191 retains 36% of the activities after treating with 2% acetic acid at 30°C for 30 min, and 45% after incubation with 4% acetic acid at 25°C for 30 min, unstable in 4% acetic acid at 30°C
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acetic acid
-
ADH from strain MSU10 shows the highest resistance to acetic acid. The enzyme retains over 90% of the original activity after 30 min incubation with 2% acetic acid at 30°C and also with 4% acetic acid at 25°C, unstable in 4% acetic acid at 30°C; ADH from strain MSU10 shows the highest resistance to acetic acid. The enzyme retains over 90% of the original activity after 30 min incubation with 2% acetic acid at 30°C and also with 4% acetic acid at 25°C, unstable in 4% acetic acid at 30°C
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acetic acid
-
ADH from strain SKU1108 retains 61% of the activities after treating with 2% acetic acid at 30°C for 30 min, and 79% after incubation with 4% acetic acid at 25°C for 30 min, unstable in 4% acetic acid at 30°C; ADH from strain SKU1108 retains 61% of the activities after treating with 2% acetic acid at 30°C for 30 min, and 79% after incubation with 4% acetic acid at 25°C for 30 min, unstable in 4% acetic acid at 30°C; ADH from strain SKU1108 retains 61% of the activities after treating with 2% acetic acid at 30°C for 30 min, and 79% after incubation with 4% acetic acid at 25°C for 30 min, unstable in 4% acetic acid at 30°C
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme from membranes by two steps of anion exchange chormatography, hydroxyapatite chromatography, and gel filtration
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native enzyme from strain IFO3191 by ultracentrifugation and anion exchange chromatography; native enzyme from strain IFO3191 by ultracentrifugation and anion exchange chromatography; native enzyme from strain IFO3191 by ultracentrifugation and anion exchange chromatography; native enzyme from strain MSU10 by ultracentrifugation and anion exchange chromatography; native enzyme from strain MSU10 by ultracentrifugation and anion exchange chromatography; native enzyme from strain SKU1108 by ultracentrifugation and anion exchange chromatography; native enzyme from strain SKU1108 by ultracentrifugation and anion exchange chromatography; native enzyme from strain SKU1108 by ultracentrifugation and anion exchange chromatography
recombinant His6-tagged enzyme from Escherichia coli strain TOP10 by ultracentrifugation, nickel affinity chromatography, ultrafiltration, and desalting gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene adhA, DNA and amino acid sequence determination and analysis, sequence comparison of the genes encoding subunit I, subunit II, and subunit III of ADHs; gene adhA, DNA and amino acid sequence determination and analysis, sequence comparison of the genes encoding subunit I, subunit II, and subunit III of ADHs; gene adhB, DNA and amino acid sequence determination and analysis, sequence comparison of the genes encoding subunit I, subunit II, and subunit III of ADHs; gene adhB, DNA and amino acid sequence determination and analysis, sequence comparison of the genes encoding subunit I, subunit II, and subunit III of ADHs; gene adhS, DNA and amino acid sequence determination and analysis, sequence comparison of the genes encoding subunit I, subunit II, and subunit III of ADHs
gene exaF, or exaA, DNA and amino acid sequence determination and analysis, functional recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain TOP10
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sequence comparisons and phylogenetic tree, real-time reverse transcriptase PCR expression analysis
sequence comparisons and phylogenetic tree, real-time reverse transcriptase PCR expression analysis
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sequence comparisons and phylogenetic tree, real-time reverse transcriptase PCR expression analysis
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sequence comparisons and phylogenetic tree, real-time reverse transcriptase PCR expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ethanol does not affect the adhS gene expression but induces PQQ-ADH activity
the enzyme is induced by diethylstilbestrol, presence of diethylstilbestrol causes a 5.2fold increase in the mRNA level of the gene encoding quinoprotein alcohol dehydrogenase
ethanol does not affect the adhS gene expression but induces PQQ-ADH activity
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ethanol does not affect the adhS gene expression but induces PQQ-ADH activity
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the enzyme is induced by diethylstilbestrol, presence of diethylstilbestrol causes a 5.2fold increase in the mRNA level of the gene encoding quinoprotein alcohol dehydrogenase
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the enzyme is induced by diethylstilbestrol, presence of diethylstilbestrol causes a 5.2fold increase in the mRNA level of the gene encoding quinoprotein alcohol dehydrogenase
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A26V
-
site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
G55D
-
site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
L18Q
-
site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
T104K
-
site-directed mutagenesis, the mutation leads to a complete loss of ethanol oxidizing ability
V107A
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site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
V36I
-
site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
V54I
-
site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
V70A
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site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
C105A/C106A
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mutation of residues forming a characteristic disulfide ring in the binding pocket of pyrroloquinoline quinone. Analysis by EPR spectroscopy shows that the disulfide ring is no prerequisite for the formation of the functionally important semiquinone form of pyrroloquinoline quinone
additional information
additional information
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construction of adhS gene disruptant and mutants. The adhS gene disruptant completely loses its PQQ-ADH activity and acetate-producing ability but retains acetic acid toleration. In contrast, this disruptant grows well, even better than the wild-type, in the ethanol containing medium even though its PQQ-ADH activity and ethanol oxidizing ability is completely lost, while NAD+-dependent ADH is induced. Random mutagenesis of adhS gene reveal that complete loss of PQQ-ADH activity and ethanol oxidizing ability are observed in the mutants lacking the 140 and 73 amino acid residues at the C-terminal, whereas the lack of 22 amino acid residues at the C-terminal affects neither the PQQ-ADH activity nor ethanol oxidizing ability, overview
additional information
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a triple mutant strain (mxaF xoxF1 xoxF2, named MDH-3), deficient in the three methanol dehydrogenases of the model methylotroph Methylobacterium extorquens AM1, is able to grow poorly with methanol if exogenous lanthanides are added to the growth medium. When the gene encoding a putative quinoprotein ethanol dehydrogenase, exaF, is mutated in the MDH-3 background, the quadruple mutant strain can no longer grow on methanol in minimal medium with added lanthanum (La3+)
additional information
Methylobacterium extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
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a triple mutant strain (mxaF xoxF1 xoxF2, named MDH-3), deficient in the three methanol dehydrogenases of the model methylotroph Methylobacterium extorquens AM1, is able to grow poorly with methanol if exogenous lanthanides are added to the growth medium. When the gene encoding a putative quinoprotein ethanol dehydrogenase, exaF, is mutated in the MDH-3 background, the quadruple mutant strain can no longer grow on methanol in minimal medium with added lanthanum (La3+)
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additional information
In the presence of the prosthetic group, expression of the Pseudomonas gene encoding the 60-kDa subunit of quinoprotein ethanol dehydrogenase in Escherichia coli results in formation of active enzyme
additional information
generation of a single deletion mutant strain of the gene coding for PedE resulting in strain GN104, and of a double mutant with deletion of both genes PedE and PedH, strain GN127; generation of a single deletion mutant strain of the gene coding for PedH resulting in strain GN116, and of a double mutant with deletion of both genes PedE and PedH, strain GN127
additional information
generation of a single deletion mutant strain of the gene coding for PedE resulting in strain GN104, and of a double mutant with deletion of both genes PedE and PedH, strain GN127; generation of a single deletion mutant strain of the gene coding for PedH resulting in strain GN116, and of a double mutant with deletion of both genes PedE and PedH, strain GN127
additional information
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generation of a single deletion mutant strain of the gene coding for PedE resulting in strain GN104, and of a double mutant with deletion of both genes PedE and PedH, strain GN127; generation of a single deletion mutant strain of the gene coding for PedH resulting in strain GN116, and of a double mutant with deletion of both genes PedE and PedH, strain GN127
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
treatment with trans-l,2-diaminocyclohexane-N,N,N',N'-tetraacetic acid at 30°C leads to an catalytically inactive apo-form. Upon incubation of the apo-form with Ca2+ and pyrroloquinoline quinone a fully active holo-enzyme is reconstituted. Incubation of apo-enzyme with Sr2+ and pyrroloquinoline quinone leads to the formation of an active Sr2+-form. The Sr2+ and the Ca2+-forms of the enzyme differ in their absorption spectra.
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
environmental protection
environmental protection
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potential application of Pseudomonas sp. strain J51 in the treatment of DES-contaminated freshwater and seawater environments
environmental protection
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potential application of Pseudomonas sp. strain J51 in the treatment of DES-contaminated freshwater and seawater environments
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