1.1.2.8: alcohol dehydrogenase (cytochrome c)
This is an abbreviated version!
For detailed information about alcohol dehydrogenase (cytochrome c), go to the full flat file.
Word Map on EC 1.1.2.8
Reaction
Synonyms
Ca2+-dependent PQQ-ADH, EC 1.1.99.8, EDH, ethanol dehydrogenase, exaA, exaF, PedE, PedH, PpADH, PP_2674, PP_2679, PQQ-ADH, PQQ-alcohol dehydrogenase, PQQ-dependent alcohol dehydrogenase, PQQ-dependent type I alcohol dehydrogenase, PQQ-DH9, pyrroloquinoline quinone ethanol dehydrogenase, pyrroloquinoline quinone-dependent alcohol dehydrogenases, pyrroloquinoline quinone-dependent dehydrogenase, pyrroloquinoline quinone-dependent quinoprotein alcohol dehydrogenase, pyrroquinoline quinone-dependent alcohol dehydrogenase, quinoprotein alcohol dehydrogenase
ECTree
1.1.2.8 alcohol dehydrogenase (cytochrome c)Advanced search results
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results (Engineering
Engineering on EC 1.1.2.8 - alcohol dehydrogenase (cytochrome c)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A26V
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site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
G55D
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site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
L18Q
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site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
T104K
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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
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site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability
V54I
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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
E408P
mutant shows a 2.3fold increased stability upon incubation at 45°C for 1 h compared with the wild-type allele
N410K
44% relative residual activities compared with 23% for the wild-type allele upon 1 h incubation at 45°C
N410S
about 30% relative residual activities compared with 23% for the wild-type allele upon 1 h incubation at 45°C
N410T
about 35% relative residual activities compared with 23% for the wild-type allele upon 1 h incubation at 45°C
R91D
41% relative residual activities compared with 23% for the wild-type allele upon 1 h incubation at 45°C
R91D/E408P
mutant shows a 3.2fold stability upon incubation at 45°C for 1 h compared with the wild-type allele
R91D/E408P/N410K
R91E
about 35% relative residual activities compared with 23% for the wild-type allele upon 1 h incubation at 45°C
R91Q
about 30% relative residual activities compared with 23% for the wild-type allele upon 1 h incubation at 45°C
additional information
R91D/E408P/N410K
mutant shows a 4.0fold increased stability upon incubation at 45°C for 1 h compared with the wild-type allele
R91D/E408P/N410K
the mutant exhibits a 7°C increase in thermal stability but also a twofold increase in residual activity upon incubation with up to 50% dimethyl sulfoxide, while showing no significant difference in enzymatic efficiency (kcat/KM)
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
Methylorubrum 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
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
additional information
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 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
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additional information
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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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