Information on EC 1.1.2.9 - 1-butanol dehydrogenase (cytochrome c)

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The expected taxonomic range for this enzyme is: Thauera butanivorans

EC NUMBER
COMMENTARY hide
1.1.2.9
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RECOMMENDED NAME
GeneOntology No.
1-butanol dehydrogenase (cytochrome c)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
butan-1-ol + 2 ferricytochrome c = butanal + 2 ferrocytochrome c + 2 H+
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
butane degradation
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SYSTEMATIC NAME
IUBMB Comments
butan-1-ol:ferricytochrome c oxidoreductase
This periplasmic quinoprotein alcohol dehydrogenase, characterized from the bacterium Thauera butanivorans, is involved in butane degradation. It contains both pyrroloquinoline quinone (PQQ) and heme c prosthetic groups. cf. EC 1.1.5.11, 1-butanol dehydrogenase (quinone).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
insertional disruption of the enzyme gene affects adversely, but does not eliminate, butane utilization
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-butanediol + ferricytochrome c
?
show the reaction diagram
-
30% activity compared to 1-butan-1-ol
-
-
?
1,2-propanediol + ferricytochrome c
?
show the reaction diagram
-
4% activity compared to 1-butan-1-ol
-
-
?
1,3-propanediol + ferricytochrome c
?
show the reaction diagram
-
5% activity compared to 1-butan-1-ol
-
-
?
1,4-butanediol + ferricytochrome c
?
show the reaction diagram
-
24% activity compared to 1-butan-1-ol
-
-
?
1,4-pentanediol + ferricytochrome c
?
show the reaction diagram
-
1% activity compared to 1-butan-1-ol
-
-
?
1-heptanol + ferricytochrome c
heptanal + ferrocytochrome c + H+
show the reaction diagram
-
31% activity compared to 1-butan-1-ol
-
-
?
1-hexanol + ferricytochrome c
hexanal + ferrocytochrome c + H+
show the reaction diagram
-
29% activity compared to 1-butan-1-ol
-
-
?
1-nonanol + ferricytochrome c
nonanal + ferrocytochrome c + H+
show the reaction diagram
-
9% activity compared to 1-butan-1-ol
-
-
?
1-octanol + ferricytochrome c
octanal + ferrocytochrome c + H+
show the reaction diagram
-
19% activity compared to 1-butan-1-ol
-
-
?
1-pentanol + ferricytochrome c
pentanal + ferrocytochrome c + H+
show the reaction diagram
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45% activity compared to 1-butan-1-ol
-
-
?
1-propanol + ferricytochrome c
propanal + ferrocytochrome c + H+
show the reaction diagram
-
66% activity compared to 1-butan-1-ol
-
-
?
2,3-butanediol + ferricytochrome c
?
show the reaction diagram
-
2% activity compared to 1-butan-1-ol
-
-
?
2,4-pentanediol + ferricytochrome c
?
show the reaction diagram
-
2% activity compared to 1-butan-1-ol
-
-
?
2-butanol + ferricytochrome c
2-butanone + ferrocytochrome c + H+
show the reaction diagram
-
9% activity compared to 1-butan-1-ol
-
-
?
2-heptanol + ferricytochrome c
2-heptanone + ferrocytochrome c + H+
show the reaction diagram
-
49% activity compared to 1-butan-1-ol
-
-
?
2-hexanol + ferricytochrome c
?
show the reaction diagram
-
56% activity compared to 1-butan-1-ol
-
-
?
2-nonanol + ferricytochrome c
2-nonanone + ferrocytochrome c + H+
show the reaction diagram
-
35% activity compared to 1-butan-1-ol
-
-
?
2-octanol + ferricytochrome c
2-octanone + ferrocytochrome c + H+
show the reaction diagram
-
42% activity compared to 1-butan-1-ol
-
-
?
2-pentanol + ferricytochrome c
2-pentanone + ferrocytochrome c + H+
show the reaction diagram
-
68% activity compared to 1-butan-1-ol
-
-
?
2-propanol + ferricytochrome c
?
show the reaction diagram
-
52% activity compared to 1-butan-1-ol
-
-
?
acetaldehyde + ferricytochrome c
?
show the reaction diagram
-
54% activity compared to 1-butan-1-ol
-
-
?
benzyl alcohol + ferricytochrome c
benzaldehyde + ferrocytochrome c + H+
show the reaction diagram
-
11% activity compared to 1-butan-1-ol
-
-
?
butan-1-ol + ferricytochrome c
butanal + ferrocytochrome c + H+
show the reaction diagram
butyraldehyde + ferricytochrome c
?
show the reaction diagram
-
78% activity compared to 1-butan-1-ol
-
-
?
ethanol + ferricytochrome c
acetaldehyde + ferrocytochrome c + H+
show the reaction diagram
-
34% activity compared to 1-butan-1-ol
-
-
?
methanol + ferricytochrome c
formaldehyde + ferrocytochrome c + H+
show the reaction diagram
-
2% activity compared to 1-butan-1-ol
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-
?
phenol + ferricytochrome c
?
show the reaction diagram
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13% activity compared to 1-butan-1-ol
-
-
?
propionaldehyde + ferricytochrome c
?
show the reaction diagram
-
61% activity compared to 1-butan-1-ol
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?
additional information
?
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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
butan-1-ol + ferricytochrome c
butanal + ferrocytochrome c + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyrroloquinoline quinone
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-
additional information
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NAD+-independent
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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calcium ions (up to 10 mM) increase the enzyme activity substantially
NH4+
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activity is increased approximately 3fold in the presence of ammonium ions (4 mM)
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
antimycin A
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12% inhibition at 1 mM
Salicylhydroxamic acid
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7% inhibition at 3 mM
additional information
-
not inhibited by cyanide (1 mM)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007
butan-1-ol
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at pH 8.0 and 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
720
butan-1-ol
Thauera butanivorans
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at pH 8.0 and 25°C
2646
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.13
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crude supernatant, at pH 8.0 and 25°C
4.8
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after 37fold purification, at pH 8.0 and 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
calculated from amino acid sequence
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
69000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 66000, SDS-PAGE; x * 70900, calculated from amino acid sequence
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 60
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the temperature range of maximum stability of the enzyme is 25-32°C, within which the loss of enzyme activity is insignificant after a 30 min incubation. In contrast, enzyme activity is decreased 77% when incubated at 60°C for the same period of time
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80, 25 mM Tris-HCl pH 8.0, more than 6 months, no loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, 4-amino-butanol affinity column chromatography, and Q-Sepharose column chromatography
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Q-Sepharose column chromatography and Superose 6 gel filtration
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme mRNA is induced when the cell's 1-butanol oxidation activity is induced