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Information on EC 1.1.2.9 - 1-butanol dehydrogenase (cytochrome c)
for references in articles please use BRENDA:EC1.1.2.9
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.2 With a cytochrome as acceptor
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 cofactors. cf. EC 1.1.5.11, 1-butanol dehydrogenase (quinone).
The expected taxonomic range for this enzyme is: Thauera butanivorans
showSynonyms
1-butanol dehydrogenase, more
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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
MetaCyc
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 cofactors. cf. EC 1.1.5.11, 1-butanol dehydrogenase (quinone).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-butanediol + ferricytochrome c
?
-
Substrates: 30% activity compared to 1-butan-1-ol
Products: -
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?
1,2-propanediol + ferricytochrome c
?
-
Substrates: 4% activity compared to 1-butan-1-ol
Products: -
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?
1,3-propanediol + ferricytochrome c
?
-
Substrates: 5% activity compared to 1-butan-1-ol
Products: -
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?
1,4-butanediol + ferricytochrome c
?
-
Substrates: 24% activity compared to 1-butan-1-ol
Products: -
Products: -
?
1,4-pentanediol + ferricytochrome c
?
-
Substrates: 1% activity compared to 1-butan-1-ol
Products: -
Products: -
?
1-heptanol + ferricytochrome c
heptanal + ferrocytochrome c + H+
-
Substrates: 31% activity compared to 1-butan-1-ol
Products: -
Products: -
?
1-hexanol + ferricytochrome c
hexanal + ferrocytochrome c + H+
-
Substrates: 29% activity compared to 1-butan-1-ol
Products: -
Products: -
?
1-nonanol + ferricytochrome c
nonanal + ferrocytochrome c + H+
-
Substrates: 9% activity compared to 1-butan-1-ol
Products: -
Products: -
?
1-octanol + ferricytochrome c
octanal + ferrocytochrome c + H+
-
Substrates: 19% activity compared to 1-butan-1-ol
Products: -
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?
1-pentanol + ferricytochrome c
pentanal + ferrocytochrome c + H+
-
Substrates: 45% activity compared to 1-butan-1-ol
Products: -
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?
1-propanol + ferricytochrome c
propanal + ferrocytochrome c + H+
-
Substrates: 66% activity compared to 1-butan-1-ol
Products: -
Products: -
?
2,3-butanediol + ferricytochrome c
?
-
Substrates: 2% activity compared to 1-butan-1-ol
Products: -
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?
2,4-pentanediol + ferricytochrome c
?
-
Substrates: 2% activity compared to 1-butan-1-ol
Products: -
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?
2-butanol + ferricytochrome c
2-butanone + ferrocytochrome c + H+
-
Substrates: 9% activity compared to 1-butan-1-ol
Products: -
Products: -
?
2-heptanol + ferricytochrome c
2-heptanone + ferrocytochrome c + H+
-
Substrates: 49% activity compared to 1-butan-1-ol
Products: -
Products: -
?
2-hexanol + ferricytochrome c
?
-
Substrates: 56% activity compared to 1-butan-1-ol
Products: -
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?
2-nonanol + ferricytochrome c
2-nonanone + ferrocytochrome c + H+
-
Substrates: 35% activity compared to 1-butan-1-ol
Products: -
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?
2-octanol + ferricytochrome c
2-octanone + ferrocytochrome c + H+
-
Substrates: 42% activity compared to 1-butan-1-ol
Products: -
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?
2-pentanol + ferricytochrome c
2-pentanone + ferrocytochrome c + H+
-
Substrates: 68% activity compared to 1-butan-1-ol
Products: -
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?
2-propanol + ferricytochrome c
?
-
Substrates: 52% activity compared to 1-butan-1-ol
Products: -
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?
acetaldehyde + ferricytochrome c
?
-
Substrates: 54% activity compared to 1-butan-1-ol
Products: -
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?
benzyl alcohol + ferricytochrome c
benzaldehyde + ferrocytochrome c + H+
-
Substrates: 11% activity compared to 1-butan-1-ol
Products: -
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?
butyraldehyde + ferricytochrome c
?
-
Substrates: 78% activity compared to 1-butan-1-ol
Products: -
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?
ethanol + ferricytochrome c
acetaldehyde + ferrocytochrome c + H+
-
Substrates: 34% activity compared to 1-butan-1-ol
Products: -
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?
methanol + ferricytochrome c
formaldehyde + ferrocytochrome c + H+
-
Substrates: 2% activity compared to 1-butan-1-ol
Products: -
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?
phenol + ferricytochrome c
?
-
Substrates: 13% activity compared to 1-butan-1-ol
Products: -
Products: -
?
propionaldehyde + ferricytochrome c
?
-
Substrates: 61% activity compared to 1-butan-1-ol
Products: -
Products: -
?
butan-1-ol + ferricytochrome c
butanal + ferrocytochrome c + H+
Substrates: -
Products: -
Products: -
?
butan-1-ol + ferricytochrome c
butanal + ferrocytochrome c + H+
-
Substrates: -
Products: -
Products: -
?
butan-1-ol + ferricytochrome c
butanal + ferrocytochrome c + H+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with 2-butanol
Products: -
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?
additional information
?
-
-
Substrates: the enzyme also exhibits ferricyanide-dependent alcohol dehydrogenase activity
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
butan-1-ol + ferricytochrome c
butanal + ferrocytochrome c + H+
Substrates: -
Products: -
Products: -
?
butan-1-ol + ferricytochrome c
butanal + ferrocytochrome c + H+
-
Substrates: -
Products: -
Products: -
?
butan-1-ol + ferricytochrome c
butanal + ferrocytochrome c + H+
-
Substrates: -
Products: -
Products: -
?
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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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 / CCUG 51053 / NBRC 103042 / IAM 12574 / Bu B1211)
691
0
75071
Swiss-Prot
other Location (Reliability: 2)
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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
EXTERNAL LINKS (specific for EC-Number 1.1.2.9)
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