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IUBMB Comments This periplasmic quinoprotein alcohol dehydrogenase, characterized from the bacterium Thauera butanivorans , is involved in butane degradation. It contains a tightly-bound pyrroloquinoline quinone (PQQ) cofactor. cf . EC 1.1.2.9 , 1-butanol dehydrogenase (cytochrome c ).
The enzyme appears in viruses and cellular organisms
Synonyms 1-butanol dehydrogenase, AdhA , BDH, BOH, MEDH-PD Cyt c551i, NAD+-independent 1-butanol dehydrogenase, PQQ-ADH, more
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NAD+-independent 1-butanol dehydrogenase
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inducible
1-butanol dehydrogenase
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1-butanol dehydrogenase
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1-butanol dehydrogenase
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1-butanol dehydrogenase
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1-butanol dehydrogenase
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AdhA
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BOH
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PQQ-ADH
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butan-1-ol + a quinone = butanal + a quinol
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MetaCyc
butane degradation
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butan-1-ol:quinone oxidoreductase
This periplasmic quinoprotein alcohol dehydrogenase, characterized from the bacterium Thauera butanivorans, is involved in butane degradation. It contains a tightly-bound pyrroloquinoline quinone (PQQ) cofactor. cf. EC 1.1.2.9, 1-butanol dehydrogenase (cytochrome c).
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1-octanol + a quinone
octanal + a quinol
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Substrates: 22% activity compared to butan-2-ol Products: -
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1-pentanol + a quinone
pentanal + a quinol
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Substrates: 34% activity compared to butan-2-ol Products: -
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1-propanol + a quinone
propanal + a quinol
2-butanol + a quinone
2-butanone + a quinol
butan-1-ol + a quinone
butanal + a quinol
butan-2-ol + a quinone
2-butanone + a quinol
butyraldehyde + a quinol
1-butanol + a quinone
butyraldehyde + a quinol
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Substrates: 25% activity compared to butan-2-ol Products: -
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ethanol + a quinone
acetaldehyde + a quinol
methanol + a quinone
formaldehyde + a quinol
octan-2-ol + a quinone
2-octanone + a quinol
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Substrates: 15% activity compared to butan-2-ol Products: -
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pentan-2-ol + a quinone
2-pentanone + a quinol
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Substrates: 61% activity compared to butan-2-ol Products: -
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propan-2-ol + a quinone
acetone + a quinol
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Substrates: 0.7% activity compared to butan-2-ol Products: -
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propionaldehyde + a quinol
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Substrates: 33% activity compared to butan-2-ol Products: -
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1-propanol + a quinone
propanal + a quinol
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Substrates: 22% activity compared to butan-2-ol Products: -
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1-propanol + a quinone
propanal + a quinol
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Substrates: 22% activity compared to butan-2-ol Products: -
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2-butanol + a quinone
2-butanone + a quinol
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Substrates: - Products: -
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2-butanol + a quinone
2-butanone + a quinol
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Substrates: - Products: -
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butan-1-ol + a quinone
butanal + a quinol
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Substrates: - Products: -
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butan-1-ol + a quinone
butanal + a quinol
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Substrates: 87% activity compared to butan-2-ol Products: -
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butan-1-ol + a quinone
butanal + a quinol
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Substrates: - Products: -
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butan-1-ol + a quinone
butanal + a quinol
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Substrates: 87% activity compared to butan-2-ol Products: -
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butan-2-ol + a quinone
2-butanone + a quinol
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Substrates: 100% activity Products: -
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butan-2-ol + a quinone
2-butanone + a quinol
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Substrates: 100% activity Products: -
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butyraldehyde + a quinol
1-butanol + a quinone
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Substrates: - Products: -
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butyraldehyde + a quinol
1-butanol + a quinone
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Substrates: - Products: -
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ethanol + a quinone
acetaldehyde + a quinol
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Substrates: 0.7% activity compared to butan-2-ol Products: -
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ethanol + a quinone
acetaldehyde + a quinol
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Substrates: 0.7% activity compared to butan-2-ol Products: -
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methanol + a quinone
formaldehyde + a quinol
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Substrates: 0.7% activity compared to butan-2-ol Products: -
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methanol + a quinone
formaldehyde + a quinol
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Substrates: 0.7% activity compared to butan-2-ol Products: -
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butan-1-ol + a quinone
butanal + a quinol
butan-1-ol + a quinone
butanal + a quinol
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Substrates: - Products: -
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butan-1-ol + a quinone
butanal + a quinol
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Substrates: - Products: -
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additional information
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NAD+-independent
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pyrroloquinoline quinone
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pyrroloquinoline quinone
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acetic acid
about 20% residual activity at 8% (v/v) acetic acid
antimycin A
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3% inhibition at 1 mM
Salicylhydroxamic acid
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5% inhibition at 3 mM
additional information
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not inhibited by cyanide (1 mM)
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0.662
2-butanol
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at pH 7.0 and 30°C
0.0017
butan-1-ol
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at pH 7.0 and 30°C
0.369
Butyraldehyde
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at pH 7.0 and 30°C
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10 - 40
more than 60% activity between 10 and 40°C, no activity at 50°C
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6.2
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calculated from amino acid sequence
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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malfunction
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insertional disruption of the enzyme gene adversely, but does not eliminate, butane utilization
malfunction
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insertional disruption of the enzyme gene adversely, but does not eliminate, butane utilization
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BOH_THABB
Thauera butanivorans (strain ATCC 43655 / DSM 2080 / JCM 20651 / CCUG 51053 / NBRC 103042 / IAM 12574 / Bu B1211)
623
0
67553
Swiss-Prot
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S6D3Q2_9GAMM
737
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81156
TrEMBL
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x * 67553, calculated from amino acid sequence
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x * 67553, calculated from amino acid sequence
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DEAE Toyopearl column chromatography, CM Toyopearl column chromatography, and hydroxyapatite column chromatography
Q-Sepharose column chromatography and Superose 6 gel filtration
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the enzyme's mRNAs is induced when the cell's 1-butanol oxidation activity is induced
the enzyme's mRNAs is induced when the cell's 1-butanol oxidation activity is induced
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the enzyme's mRNAs is induced when the cell's 1-butanol oxidation activity is induced
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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, Thauera butanivorans ATCC 43655
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Treek, J.; Matsushita, K.
A unique enzyme of acetic acid bacteria, PQQ-dependent alcohol dehydrogenase, is also present in Frateuria aurantia
Appl. Microbiol. Biotechnol.
97
7369-7376
2013
Frateuria aurantia (S6D3Q2), Frateuria aurantia LMG 1558T (S6D3Q2)
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
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