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Information on EC 1.1.2.B3 - quinoprotein methanol dehydrogenase (cytochrome c559) and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9Z4J7

for references in articles please use BRENDA:EC1.1.2.B3
preliminary BRENDA-supplied EC number
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Pseudomonas aeruginosa
UNIPROT: Q9Z4J7 not found.
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Pseudomonas
Synonyms
exaA, More, PedE, PedH, PQQ-alcohol dehydrogenase, PQQ-linked alcohol dehydrogenase, pyrroloquinoline quinone -dependent quinoprotein ethanol dehydrogenase, QEDH, quinoprotein ethanol dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pyrroloquinoline quinone -dependent quinoprotein ethanol dehydrogenase
-
quinoprotein ethanol dehydrogenase
-
SYSTEMATIC NAME
IUBMB Comments
methanol:ferricytochrome c550 oxidoreductase
-
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
ethanol + ferricytochrome c550
acetaldehyde + ferrocytochrome c550
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
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
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
-
-
?
ethanol + ferricytochrome c550
acetaldehyde + ferrocytochrome c550
show the reaction diagram
regulation of ethanol-oxidation system in Pseudomonas aeruginosa
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyrroloquinoline quinone
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
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
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
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
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
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PROTEIN VARIANTS
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
construction of four exaAB mutants, phenotypes, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
exaAB, DNA and amino acid sequence determination and analysis, exaA encodes the enzyme, while exaB encodes a cytochrome 550
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schobert, M.; Goerisch, H.
A soluble two-component regulatory system controls expression of quinoprotein ethanol dehydrogenase (QEDH) but not expression of cytochrome c(550) of the ethanol-oxidation system in Pseudomonas aeruginosa
Microbiology
147
363-372
2001
Pseudomonas aeruginosa (Q9Z4J7)
Manually annotated by BRENDA team
Mennenga, B.; Kay, C.W.; Goerisch, H.
Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the unusual disulfide ring formed by adjacent cysteine residues is essential for efficient electron transfer to cytochrome c550
Arch. Microbiol.
191
361-367
2009
Pseudomonas aeruginosa (Q9Z4J7)
Manually annotated by BRENDA team