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Information on EC 1.1.2.9 - 1-butanol dehydrogenase (cytochrome c)
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1.1.2.9 1-butanol dehydrogenase (cytochrome c)IUBMB Comments
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).
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The expected taxonomic range for this enzyme is: Thauera butanivorans
Synonyms
1-butanol dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-butanol dehydrogenase
BDH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
butan-1-ol + 2 ferricytochrome c = butanal + 2 ferrocytochrome c + 2 H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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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).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-butanediol + ferricytochrome c
?
-
30% activity compared to 1-butan-1-ol
-
-
?
1,2-propanediol + ferricytochrome c
?
-
4% activity compared to 1-butan-1-ol
-
-
?
1,3-propanediol + ferricytochrome c
?
-
5% activity compared to 1-butan-1-ol
-
-
?
1,4-butanediol + ferricytochrome c
?
-
24% activity compared to 1-butan-1-ol
-
-
?
1,4-pentanediol + ferricytochrome c
?
-
1% activity compared to 1-butan-1-ol
-
-
?
1-heptanol + ferricytochrome c
heptanal + ferrocytochrome c + H+
-
31% activity compared to 1-butan-1-ol
-
-
?
1-hexanol + ferricytochrome c
hexanal + ferrocytochrome c + H+
-
29% activity compared to 1-butan-1-ol
-
-
?
1-nonanol + ferricytochrome c
nonanal + ferrocytochrome c + H+
-
9% activity compared to 1-butan-1-ol
-
-
?
1-octanol + ferricytochrome c
octanal + ferrocytochrome c + H+
-
19% activity compared to 1-butan-1-ol
-
-
?
1-pentanol + ferricytochrome c
pentanal + ferrocytochrome c + H+
-
45% activity compared to 1-butan-1-ol
-
-
?
1-propanol + ferricytochrome c
propanal + ferrocytochrome c + H+
-
66% activity compared to 1-butan-1-ol
-
-
?
2,3-butanediol + ferricytochrome c
?
-
2% activity compared to 1-butan-1-ol
-
-
?
2,4-pentanediol + ferricytochrome c
?
-
2% activity compared to 1-butan-1-ol
-
-
?
2-butanol + ferricytochrome c
2-butanone + ferrocytochrome c + H+
-
9% activity compared to 1-butan-1-ol
-
-
?
2-heptanol + ferricytochrome c
2-heptanone + ferrocytochrome c + H+
-
49% activity compared to 1-butan-1-ol
-
-
?
2-hexanol + ferricytochrome c
?
-
56% activity compared to 1-butan-1-ol
-
-
?
2-nonanol + ferricytochrome c
2-nonanone + ferrocytochrome c + H+
-
35% activity compared to 1-butan-1-ol
-
-
?
2-octanol + ferricytochrome c
2-octanone + ferrocytochrome c + H+
-
42% activity compared to 1-butan-1-ol
-
-
?
2-pentanol + ferricytochrome c
2-pentanone + ferrocytochrome c + H+
-
68% activity compared to 1-butan-1-ol
-
-
?
2-propanol + ferricytochrome c
?
-
52% activity compared to 1-butan-1-ol
-
-
?
acetaldehyde + ferricytochrome c
?
-
54% activity compared to 1-butan-1-ol
-
-
?
benzyl alcohol + ferricytochrome c
benzaldehyde + ferrocytochrome c + H+
-
11% activity compared to 1-butan-1-ol
-
-
?
butyraldehyde + ferricytochrome c
?
-
78% activity compared to 1-butan-1-ol
-
-
?
ethanol + ferricytochrome c
acetaldehyde + ferrocytochrome c + H+
-
34% activity compared to 1-butan-1-ol
-
-
?
methanol + ferricytochrome c
formaldehyde + ferrocytochrome c + H+
-
2% activity compared to 1-butan-1-ol
-
-
?
phenol + ferricytochrome c
?
-
13% activity compared to 1-butan-1-ol
-
-
?
propionaldehyde + ferricytochrome c
?
-
61% activity compared to 1-butan-1-ol
-
-
?
butan-1-ol + ferricytochrome c
butanal + ferrocytochrome c + H+
-
-
-
-
?
butan-1-ol + ferricytochrome c
butanal + ferrocytochrome c + H+
-
-
-
?
butan-1-ol + ferricytochrome c
butanal + ferrocytochrome c + H+
-
-
-
-
?
additional information
?
-
-
the enzyme also exhibits ferricyanide-dependent alcohol dehydrogenase activity
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
butan-1-ol + ferricytochrome c
butanal + ferrocytochrome c + H+
-
-
-
-
?
butan-1-ol + ferricytochrome c
butanal + ferrocytochrome c + H+
-
-
-
?
butan-1-ol + ferricytochrome c
butanal + ferrocytochrome c + H+
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
calcium ions (up to 10 mM) increase the enzyme activity substantially
NH4+
-
activity is increased approximately 3fold in the presence of ammonium ions (4 mM)
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
insertional disruption of the enzyme gene affects adversely, but does not eliminate, butane utilization
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BDH_THABB
Thauera butanivorans (strain ATCC 43655 / DSM 2080 / JCM 20651 / NBRC 103042 / IAM 12574 / Bu B1211)
691
0
75071
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
66000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 60
-
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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme mRNA is induced when the cell's 1-butanol oxidation activity is induced
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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 (Q9AF95)
brenda
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, Thauera butanivorans ATCC 43655
brenda
Vangnai, A.; Sayavedra-Soto, L.; Arp, D.
Roles for the two 1-butanol dehydrogenases of Pseudomonas butanovora in butane and 1-butanol metabolism
J. Bacteriol.
184
4343-4350
2002
Thauera butanivorans, Thauera butanivorans ATCC 43655
brenda
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Release 2023.1 (January 2023)
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