Information on EC 1.1.2.8 - alcohol dehydrogenase (cytochrome c)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.2.8
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RECOMMENDED NAME
GeneOntology No.
alcohol dehydrogenase (cytochrome c)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a primary alcohol + 2 ferricytochrome c = an aldehyde + 2 ferrocytochrome c + 2 H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of secondary metabolites
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Chloroalkane and chloroalkene degradation
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Glycolysis / Gluconeogenesis
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Metabolic pathways
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Microbial metabolism in diverse environments
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ethanol + 2 cytochrome c
ethanal + 2 reduced cytochrome c
show the reaction diagram
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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
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ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
show the reaction diagram
ethanol + N,N,N',N'-tetramethyl-p-phenylenediamine
ethanal + ?
show the reaction diagram
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i.e. Wurster's Blue
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?
ethanol + oxidized 2,6-dichlorophenolindophenol
ethanal + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
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
ethanol + 2 ferricytochrome c
ethanal + 2 ferrocytochrome c
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c
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prosthetic groups, four per enzyme
pyrroloquinoline quinone
additional information
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one [2Fe-2S] cluster per enzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
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one [2Fe-2S] cluster per enzyme
Sr2+
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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.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ethanol
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does not affect the adhS gene expression but induces PQQ-ADH activity
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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pH 9.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
assay at; assay at; assay at; assay at; assay at; assay at; assay at; assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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1 * 72000 + 1 * 45000, inactive enzyme form, SDS-PAGE; 2 * 72000 + 2 * 45000, dimer of dimers, active enzyme form, SDS-PAGE
72000
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1 * 72000 + 1 * 45000, inactive enzyme form, SDS-PAGE; 2 * 72000 + 2 * 45000, dimer of dimers, active enzyme form, SDS-PAGE
115000
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inactive enzyme form, native PAGE
120000
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inactive enzyme form, gel filtration
136000
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gel filtration
330000
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active enzyme form, gel filtration
345000
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active enzyme form, native PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
1 * 60000 + 1 * 9000, SDS-PAGE
heterodimer
heterotetramer
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
sequence contains a signal peptide of 34 residues
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
diffraction to beyond 2.5 A, space group R3
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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 hide
LITERATURE
acetic acid
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
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ethanol does not affect the adhS gene expression but induces PQQ-ADH activity
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
additional information
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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Show AA Sequence (199 entries)
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