| pubmed-article:2933391 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2933391 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:2933391 | lifeskim:mentions | umls-concept:C1264774 | lld:lifeskim |
| pubmed-article:2933391 | lifeskim:mentions | umls-concept:C0080194 | lld:lifeskim |
| pubmed-article:2933391 | lifeskim:mentions | umls-concept:C0025519 | lld:lifeskim |
| pubmed-article:2933391 | lifeskim:mentions | umls-concept:C0001942 | lld:lifeskim |
| pubmed-article:2933391 | lifeskim:mentions | umls-concept:C0068005 | lld:lifeskim |
| pubmed-article:2933391 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:2933391 | pubmed:dateCreated | 1986-1-3 | lld:pubmed |
| pubmed-article:2933391 | pubmed:abstractText | Multiple alcohol dehydrogenases (ADH) were demonstrated in Acinetobacter sp. strain HO1-N. ADH-A and ADH-B were distinguished on the basis of electrophoretic mobility, pyridine nucleotide cofactor requirement, and substrate specificity. ADH-A is a soluble, NAD-linked, inducible ethanol dehydrogenase (EDH) exhibiting an apparent Km for ethanol of 512 microM and a Vmax of 138 nmol/min. An ethanol-negative mutant (Eth1) was isolated which contained 6.5% of wild-type EDH activity and was deficient in ADH-A. Eth1 exhibited normal growth on hexadecane and hexadecanol. A second ethanol-negative mutant (Eth3) was acetaldehyde dehydrogenase (ALDH) deficient, having 12.5% of wild-type ALDH activity. Eth3 had threefold-higher EDH activity than the wild-type strain. ALDH is a soluble, NAD-linked, ethanol-inducible enzyme which exhibited an apparent Km for acetaldehyde of 50 microM and a Vmax of 183 nmol/min. Eth3 exhibited normal growth on hexadecane, hexadecanol, and fatty aldehyde. ADH-B is a soluble, constitutive, NADP-linked ADH which was active with medium-chain-length alcohols. Hexadecanol dehydrogenase (HDH), a soluble and membrane-bound, NAD-linked ADH, was induced 5- to 11-fold by growth on hexadecane or hexadecanol. HDH exhibited apparent Kms for hexadecanol of 1.6 and 2.8 microM in crude extracts derived from hexadecane- and hexadecanol-grown cells, respectively. HDH was distinct from ADH-A and ADH-B, since HDH and ADH-A were not coinduced; Eth1 had wild-type levels of HDH; and HDH requires NAD, while ADH-B requires NADP. NAD- and NADP-independent HDH activity was not detected in the soluble or membrane fraction of extracts derived from hexadecane- or hexadecanol-grown cells. NAD-linked HDH appears to possess a functional role in hexadecane and hexadecanol dissimilation. | lld:pubmed |
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| pubmed-article:2933391 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2933391 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2933391 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2933391 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2933391 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2933391 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:2933391 | pubmed:author | pubmed-author:FinnertyW RWR | lld:pubmed |
| pubmed-article:2933391 | pubmed:author | pubmed-author:SingerM EME | lld:pubmed |
| pubmed-article:2933391 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2933391 | pubmed:volume | 164 | lld:pubmed |
| pubmed-article:2933391 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2933391 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2933391 | pubmed:pagination | 1017-24 | lld:pubmed |
| pubmed-article:2933391 | pubmed:dateRevised | 2010-9-10 | lld:pubmed |
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| pubmed-article:2933391 | pubmed:meshHeading | pubmed-meshheading:2933391-... | lld:pubmed |
| pubmed-article:2933391 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:2933391 | pubmed:articleTitle | Alcohol dehydrogenases in Acinetobacter sp. strain HO1-N: role in hexadecane and hexadecanol metabolism. | lld:pubmed |
| pubmed-article:2933391 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2933391 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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