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Information on EC 1.2.5.2 - aldehyde dehydrogenase (quinone) and Organism(s) Thauera butanivorans and UniProt Accession Q9AGW3

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EC Tree
IUBMB Comments
Wide specificity; acts on straight-chain aldehydes up to C10, aromatic aldehydes, glyoxylate and glyceraldehyde. The enzymes contains a PQQ cofactor and multiple hemes that deliver the electrons to the membrane quinone pool.
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Thauera butanivorans
UNIPROT: Q9AGW3
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The taxonomic range for the selected organisms is: Thauera butanivorans
The enzyme appears in selected viruses and cellular organisms
Synonyms
adh iib, adh iig, pqq-aldh, swit_4395, formaldehyde-oxidizing enzyme, pqq-alddh, tetrahydrofurfuryl alcohol dehydrogenase, pyrroloquinoline quinone-dependent aldehyde dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NAD+-independent, PQQ-containing alcohol dehydrogenase
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aldehyde dehydrogenase (acceptor)
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-
-
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ALDH
-
-
-
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dehydrogenase, aldehyde (acceptor)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
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-
-
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reduction
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-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
aldehyde:quinone oxidoreductase
Wide specificity; acts on straight-chain aldehydes up to C10, aromatic aldehydes, glyoxylate and glyceraldehyde. The enzymes contains a PQQ cofactor and multiple hemes that deliver the electrons to the membrane quinone pool.
CAS REGISTRY NUMBER
COMMENTARY hide
75536-77-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
butyraldehyde + 2,6-dichlorophenolindophenol
butanoate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
?
propionaldehyde + 2,6-dichlorophenolindophenol
propanoate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
30% of the activity with 2-butanol
-
-
?
1-butanol + acceptor
butanal + reduced acceptor
show the reaction diagram
-
the NAD+-independent inducible 1-butanol dehydrogenase, a quinohemoprotein, is responsible for 1-butanol oxidation in the butane metabolism pathway
-
-
?
acetaldehyde + 2,6-dichlorophenolindophenol
acetate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
butyraldehyde + 2,6-dichlorophenolindophenol
butanoate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
propionaldehyde + 2,6-dichlorophenolindophenol
propanoate + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
additional information
?
-
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
1-butanol + acceptor
butanal + reduced acceptor
show the reaction diagram
-
the NAD+-independent inducible 1-butanol dehydrogenase, a quinohemoprotein, is responsible for 1-butanol oxidation in the butane metabolism pathway
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-
?
additional information
?
-
the NAD+-independent PQQ alcohol dehydrogenase BOH (a quinoprotein) is linked to butane metabolism in conjunction with BDH (a quinohemoprotein)
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyrroloquinoline quinone
BOH is a quinoprotein
heme c
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0.25 mol of heme per mol of enzyme
pyrroloquinoline quinone
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PQQ, 1.0 mol of PQQ per mol of enzyme
additional information
BOH contains no heme c
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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highly activating
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NH4+
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3fold activation at 4 mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007
1-butanol
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0019
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lactate-grown cell extract
0.0044
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2-butanol-grown cell extract
0.0106
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1-butanol-grown cell extract
4.8
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purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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phenazine methosulfate/2,6-dichlorophenolindophenol-dependent activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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phenazine methosulfate/2,6-dichlorophenolindophenol-dependent activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
1-butanol dehydrogenase, BOH; strain ATCC 43655, gene boh
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
BOH contains the periplasm 29-residue leader sequence
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
67553
x * 67553, BOH, calculated from sequence
66000
-
1 * 66000, SDS-PAGE
69000
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gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 67553, BOH, calculated from sequence
monomer
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1 * 66000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
insertional disruption of boh affects, but not fully eliminates butane utilization in the mutant organism, the double boh/bdh mutant with both genes boh and bdh inactivated is unable to grow on butane or 1-butanol, but does, when grown in citrate and incubated in butane, develop butane oxidation capability and accumulates 1-butanol, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 32
-
purified enzyme, maximally stable within this range
60
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30 min, purified enzyme, loss of 77% activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, purified enzyme, 25 mM Tris-HCl, pH 8.0, stable for more than 6 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 37fold to near homogeneity by ammonium sulfate fractionation and anion exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene boh, DNA and amino acid sequence determination and analysis
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
Ca2+ ions facilitate the reconstitution of inactive apoenzyme
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vangnai, A.S.; Arp, D.J.; Sayavedra-Soto, L.A.
Two distinct alcohol dehydrogenases participate in butane metabolism by Pseudomonas butanovora
J. Bacteriol.
184
1916-1924
2002
Thauera butanivorans (Q9AGW3)
Manually annotated by BRENDA team
Vangnai, A.S.; Arp, D.J.
An inducible 1-butanol dehydrogenase, a quinohaemoprotein, is involved in the oxidation of butane by Pseudomonas butanovora
Microbiology
147
745-756
2001
Thauera butanivorans
Manually annotated by BRENDA team