Information on EC 1.1.2.B3 - quinoprotein methanol dehydrogenase (cytochrome c559)

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The expected taxonomic range for this enzyme is: Pseudomonas

EC NUMBER
COMMENTARY hide
1.1.2.B3
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
quinoprotein methanol dehydrogenase (cytochrome c559)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alcohol + 2 cytochrome c550 = aldehyde + 2 reduced cytochrome c550 + 2 H+
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
methanol:ferricytochrome c550 oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-propanediol + acceptor
? + reduced acceptor
show the reaction diagram
artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol
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?
1-butanol + acceptor
butanal + reduced acceptor
show the reaction diagram
artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol
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?
1-propanol + acceptor
propanal + reduced acceptor
show the reaction diagram
artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol
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?
2-propanol + acceptor
2-propanone + reduced acceptor
show the reaction diagram
artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol
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?
alcohol + cytochrome c550
aldehyde + reduced cytochrome c550
show the reaction diagram
the unusual disulfide ring between the adjacent cysteine residues C105 and C106 is essential for efficient electron transfer at pH 7 from quinoprotein ethanol dehydrogenase to its natural electron acceptor cytochrome c550
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?
ethanol + acceptor
acetaldehyde + reduced acceptor
show the reaction diagram
artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol
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-
?
ethanol + ferricytochrome c550
acetaldehyde + ferrocytochrome c550
show the reaction diagram
phenylethanol + ferricytochrome c
phenylacetaldehyde + ferrocytochrome c
show the reaction diagram
PedH catalyzes a step in the aerobic transformation of 2-phenylethylamine and 2-phenylethanol. PedH does not belong to the class of PQQ-dependent alcohol dehydrogenases containing a c-type cytochrome heme domain, but to others that transfer electrons to a separate soluble c-type cytochrome
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alcohol + cytochrome c550
aldehyde + reduced cytochrome c550
show the reaction diagram
Q9Z4J7
the unusual disulfide ring between the adjacent cysteine residues C105 and C106 is essential for efficient electron transfer at pH 7 from quinoprotein ethanol dehydrogenase to its natural electron acceptor cytochrome c550
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?
ethanol + ferricytochrome c550
acetaldehyde + ferrocytochrome c550
show the reaction diagram
Q9Z4J7
regulation of ethanol-oxidation system in Pseudomonas aeruginosa
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?
phenylethanol + ferricytochrome c
phenylacetaldehyde + ferrocytochrome c
show the reaction diagram
B1N7J0, B1N7J5
PedH catalyzes a step in the aerobic transformation of 2-phenylethylamine and 2-phenylethanol. PedH does not belong to the class of PQQ-dependent alcohol dehydrogenases containing a c-type cytochrome heme domain, but to others that transfer electrons to a separate soluble c-type cytochrome
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyrroloquinoline quinone
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Amine
the enzymatic activity of the mutant enzyme in the artificial dye test with N-methylphenazonium methyl sulfate (PMS) and 2,6-dichlorophenol indophenol (DCPIP) at pH 9 does not depend on an activating amine which is essential for wild type activity under these condition
ethylamine
5 mM, wild-type enzyme shows strict dependence on an activator
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21 - 266
1,3-Propanediol
0.43 - 12
1-butanol
0.062 - 3.8
1-propanol
1.4 - 1.5
2-propanol
0.012 - 12
ethanol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11
substrate: 2-propanol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, wild-type enzyme; substrate: ethanol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, wild-type enzyme
15
substrate: 1-propanol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, wild-type enzyme
20
substrate: ethanol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, mutant enzyme C105A/C106A
40
substrate: 1,3-propanediol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, wild-type enzyme
42
substrate: 1-butanol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, wild-type enzyme
52
substrate: 1-propanol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, mutant enzyme C105A/C106A
94
substrate: 2-propanol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, mutant enzyme C105A/C106A
224
substrate: 1,3-propanediol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, mutant enzyme C105A/C106A
461
substrate: 1-butanol, pH 9 in the artificial dye test at fixed concentrations of N-methylphenazonium methyl sulfate and 2,6-dichlorophenol indophenol in the presence of 5 mM ethylamine, mutant enzyme C105A/C106A
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
64870
x * 64870, PedH, sequence calculation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 64870, PedH, sequence calculation
additional information
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
exaAB, DNA and amino acid sequence determination and analysis, exaA encodes the enzyme, while exaB encodes a cytochrome 550
gene pedE, DNA and amino acid sequence determination and analysis; gene pedH, DNA and amino acid sequence determination and analysis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C105A/C106A
all pyrroloquinoline quinone-dependent alcohol dehydrogenases contain an unusual disulfide ring formed between adjacent cysteine residues. A mutant enzyme that is lacking this structure is generated by replacing Cys105 and Cys106 with Ala. Heterologously expressed C105A/C106A apoenzyme is successfully converted to enzymatic active holo-enzyme by incorporation of its cofactor pyrroloquinoline quinone (PQQ) in the presence of Ca2+. The enzymatic activity of the mutant enzyme in the artificial dye test with N-methylphenazonium methyl sulfate (PMS) and 2,6-dichlorophenol indophenol (DCPIP) at pH 9 does not depend on an activating amine which is essential for wild type activity under these conditions. The mutant enzyme shows increased Michaelis constants for primary alcohols, while the affinity for the secondary alcohol 2-propanol is unaltered. For all substrates tested the specific activity of the mutant enzyme in the artificial dye test is higher than that found for wild type enzyme. In the ferricyanide test with the natural electron acceptor cytochrome c550 the activity of mutant Cys105Ala/Cys106Ala is 15fold lower than that of wild type enzyme
additional information