| pubmed-article:572296 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:572296 | lifeskim:mentions | umls-concept:C0752019 | lld:lifeskim |
| pubmed-article:572296 | lifeskim:mentions | umls-concept:C0752025 | lld:lifeskim |
| pubmed-article:572296 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:572296 | lifeskim:mentions | umls-concept:C0025617 | lld:lifeskim |
| pubmed-article:572296 | lifeskim:mentions | umls-concept:C0150141 | lld:lifeskim |
| pubmed-article:572296 | lifeskim:mentions | umls-concept:C2828366 | lld:lifeskim |
| pubmed-article:572296 | lifeskim:mentions | umls-concept:C1705851 | lld:lifeskim |
| pubmed-article:572296 | lifeskim:mentions | umls-concept:C1555707 | lld:lifeskim |
| pubmed-article:572296 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:572296 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:572296 | lifeskim:mentions | umls-concept:C2348205 | lld:lifeskim |
| pubmed-article:572296 | lifeskim:mentions | umls-concept:C2752151 | lld:lifeskim |
| pubmed-article:572296 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:572296 | pubmed:dateCreated | 1979-9-25 | lld:pubmed |
| pubmed-article:572296 | pubmed:abstractText | 1. The methane mono-oxygenase from Methylosinus trichosporium OB3b was soluble. The only suitable electron donor was NAD(P)H, neither sodium L-ascorbate nor electrons derived from the oxidation of methanol could substitute for NAD(P)H. Evidence is presented for the existence of an NAD+-linked formaldehyde dehydrogenase. 2. Mono-oxygenase activity was not inhibited by a range of potential inhibitors including potassium cyanide, amytal, carbon monoxide or various metal-chelating agents, although 8-hydroxyquinoline and ethyne were effective in this respect. 3. Although the enzyme preparations were unstable on storage, the crude extract could be resolved into two components by ion-exchange chromatography. Activity could be restored to one of the components on addition of purified components from Methylococcus capsulatus (Bath). 4. Cross-reactivity of mono-oxygenase components and other similarities between the enzymes from M. trichosporium and M. capsulatus are discussed. The properties of the M. trichosporium methane mono-oxygenase reported here are contrasted with the properties of the same enzyme reported by others. | lld:pubmed |
| pubmed-article:572296 | pubmed:language | eng | lld:pubmed |
| pubmed-article:572296 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:572296 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:572296 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:572296 | pubmed:month | May | lld:pubmed |
| pubmed-article:572296 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:572296 | pubmed:author | pubmed-author:DaltonHH | lld:pubmed |
| pubmed-article:572296 | pubmed:author | pubmed-author:MichalováCC | lld:pubmed |
| pubmed-article:572296 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:572296 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:572296 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:572296 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:572296 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:572296 | pubmed:pagination | 205-12 | lld:pubmed |
| pubmed-article:572296 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
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| pubmed-article:572296 | pubmed:meshHeading | pubmed-meshheading:572296-A... | lld:pubmed |
| pubmed-article:572296 | pubmed:year | 1979 | lld:pubmed |
| pubmed-article:572296 | pubmed:articleTitle | Properties of the methane mono-oxygenase from extracts of Methylosinus trichosporium OB3b and evidence for its similarity to the enzyme from Methylococcus capsulatus (Bath). | lld:pubmed |
| pubmed-article:572296 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:572296 | pubmed:publicationType | Comparative Study | lld:pubmed |
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