Enzymes
| UniProtKB help_outline | 1 proteins |
| Enzyme class help_outline |
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- Name help_outline a quinone Identifier CHEBI:132124 Charge 0 Formula C6O2R4 SMILEShelp_outline O=C1C(*)=C(*)C(=O)C(*)=C1* 2D coordinates Mol file for the small molecule Search links Involved in 127 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline butan-1-ol Identifier CHEBI:28885 (Beilstein: 969148; CAS: 71-36-3) help_outline Charge 0 Formula C4H10O InChIKeyhelp_outline LRHPLDYGYMQRHN-UHFFFAOYSA-N SMILEShelp_outline CCCCO 2D coordinates Mol file for the small molecule Search links Involved in 12 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a quinol Identifier CHEBI:24646 Charge 0 Formula C6H2O2R4 SMILEShelp_outline OC1=C(*)C(*)=C(O)C(*)=C1* 2D coordinates Mol file for the small molecule Search links Involved in 238 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline butanal Identifier CHEBI:15743 (CAS: 123-72-8) help_outline Charge 0 Formula C4H8O InChIKeyhelp_outline ZTQSAGDEMFDKMZ-UHFFFAOYSA-N SMILEShelp_outline [H]C(=O)CCC 2D coordinates Mol file for the small molecule Search links Involved in 15 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:49808 | RHEA:49809 | RHEA:49810 | RHEA:49811 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Roles for the two 1-butanol dehydrogenases of Pseudomonas butanovora in butane and 1-butanol metabolism.
Vangnai A.S., Sayavedra-Soto L.A., Arp D.J.
Pseudomonas butanovora grown on butane or 1-butanol expresses two 1-butanol dehydrogenases, a quinoprotein (BOH) and a quinohemoprotein (BDH). BOH exhibited high affinity towards 1-butanol (K(m) = 1.7 +/-0.2 microM). BOH also oxidized butyraldehyde and 2-butanol (K(m) = 369 +/-85 microM and K(m) = ... >> More
Pseudomonas butanovora grown on butane or 1-butanol expresses two 1-butanol dehydrogenases, a quinoprotein (BOH) and a quinohemoprotein (BDH). BOH exhibited high affinity towards 1-butanol (K(m) = 1.7 +/-0.2 microM). BOH also oxidized butyraldehyde and 2-butanol (K(m) = 369 +/-85 microM and K(m) = 662 +/-98 microM, respectively). The mRNA induction profiles of BOH and BDH at three different levels of 1-butanol, a nontoxic level (0.1 mM), a growth-supporting level (2 mM), and a toxic level (40 mM), were similar. When cells were grown in citrate-containing medium in the presence of different levels of 1-butanol, wild-type P. butanovora could tolerate higher levels of 1-butanol than the P. butanovora boh::tet strain and the P. butanovora bdh::kan strain. A model is proposed in which the electrons from 1-butanol oxidation follow a branched electron transport chain. BOH may be coupled to ubiquinone, with the electrons being transported to a cyanide-sensitive terminal oxidase. In contrast, electrons from BDH may be transferred to a terminal oxidase that is less sensitive to cyanide. The former pathway may function primarily in energy generation, while the latter may be more important in the detoxification of 1-butanol. << Less
J. Bacteriol. 184:4343-4350(2002) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Two distinct alcohol dehydrogenases participate in butane metabolism by Pseudomonas butanovora.
Vangnai A.S., Arp D.J., Sayavedra-Soto L.A.
The involvement of two primary alcohol dehydrogenases, BDH and BOH, in butane utilization in Pseudomonas butanovora (ATCC 43655) was demonstrated. The genes coding for BOH and BDH were isolated and characterized. The deduced amino acid sequence of BOH suggests a 67-kDa alcohol dehydrogenase contai ... >> More
The involvement of two primary alcohol dehydrogenases, BDH and BOH, in butane utilization in Pseudomonas butanovora (ATCC 43655) was demonstrated. The genes coding for BOH and BDH were isolated and characterized. The deduced amino acid sequence of BOH suggests a 67-kDa alcohol dehydrogenase containing pyrroloquinoline quinone (PQQ) as cofactor and in the periplasm (29-residue leader sequence). The deduced amino acid sequence of BDH is consistent with a 70.9-kDa, soluble, periplasmic (37-residue leader sequence) alcohol dehydrogenase containing PQQ and heme c as cofactors. BOH and BDH mRNAs were induced whenever the cell's 1-butanol oxidation activity was induced. When induced with butane, the gene for BOH was expressed earlier than the gene for BDH. Insertional disruption of bdh or boh affected adversely, but did not eliminate, butane utilization by P. butanovora. The P. butanovora mutant with both genes boh and bdh inactivated was unable to grow on butane or 1-butanol. These cells, when grown in citrate and incubated in butane, developed butane oxidation capability and accumulated 1-butanol. The enzyme activity of BOH was characterized in cell extracts of the P. butanovora strain with bdh disrupted. Unlike BDH, BOH oxidized 2-butanol. The results support the involvement of two distinct NAD(+)-independent, PQQ-containing alcohol dehydrogenases, BOH (a quinoprotein) and BDH (a quinohemoprotein), in the butane oxidation pathway of P. butanovora. << Less
J. Bacteriol. 184:1916-1924(2002) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.