| pubmed-article:911318 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:911318 | lifeskim:mentions | umls-concept:C0033808 | lld:lifeskim |
| pubmed-article:911318 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:911318 | lifeskim:mentions | umls-concept:C0016762 | lld:lifeskim |
| pubmed-article:911318 | lifeskim:mentions | umls-concept:C0040005 | lld:lifeskim |
| pubmed-article:911318 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:911318 | lifeskim:mentions | umls-concept:C1705920 | lld:lifeskim |
| pubmed-article:911318 | lifeskim:mentions | umls-concept:C1156694 | lld:lifeskim |
| pubmed-article:911318 | lifeskim:mentions | umls-concept:C1548602 | lld:lifeskim |
| pubmed-article:911318 | lifeskim:mentions | umls-concept:C0667253 | lld:lifeskim |
| pubmed-article:911318 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:911318 | pubmed:dateCreated | 1977-11-30 | lld:pubmed |
| pubmed-article:911318 | pubmed:abstractText | 1. The route of l-threonine degradation was studied in four strains of the genus Pseudomonas able to grow on the amino acid and selected because of their high l-threonine aldolase activity. Growth and manometric results were consistent with the cleavage of l-threonine to acetaldehyde+glycine and their metabolism via acetate and serine respectively. 2. l-Threonine aldolases in these bacteria exhibited pH optima in the range 8.0-8.7 and K(m) values for the substrate of 5-10mm. Extracts exhibited comparable allo-l-threonine aldolase activities, K(m) values for this substrate being 14.5-38.5mm depending on the bacterium. Both activities were essentially constitutive. Similar activity ratios in extracts, independent of growth conditions, suggested a single enzyme. The isolate Pseudomonas D2 (N.C.I.B. 11097) represents the best source of the enzyme known. 3. Extracts of all the l-threonine-grown pseudomonads also possessed a CoA-independent aldehyde dehydrogenase, the synthesis of which was induced, and a reversible alcohol dehydrogenase. The high acetaldehyde reductase activity of most extracts possibly resulted in the underestimation of acetaldehyde dehydrogenase. 4. l-Serine dehydratase formation was induced by growth on l-threonine or acetate+glycine. Constitutively synthesized l-serine hydroxymethyltransferase was detected in extracts of Pseudomonas strains D2 and F10. The enzyme could not be detected in strains A1 and N3, probably because of a highly active ;formaldehyde-utilizing' system. 5. Ion-exchange and molecular exclusion chromatography supported other evidence that l-threonine aldolase and allo-l-threonine aldolase activities were catalysed by the same enzyme but that l-serine hydroxymethyltransferase was distinct and different. These results contrast with the specificities of some analogous enzymes of mammalian origin. | lld:pubmed |
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| pubmed-article:911318 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:911318 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:911318 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:911318 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:911318 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:911318 | pubmed:author | pubmed-author:TurnerJ MJM | lld:pubmed |
| pubmed-article:911318 | pubmed:author | pubmed-author:BellS CSC | lld:pubmed |
| pubmed-article:911318 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:911318 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:911318 | pubmed:volume | 166 | lld:pubmed |
| pubmed-article:911318 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:911318 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:911318 | pubmed:pagination | 209-16 | lld:pubmed |
| pubmed-article:911318 | pubmed:dateRevised | 2010-9-3 | lld:pubmed |
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| pubmed-article:911318 | pubmed:year | 1977 | lld:pubmed |
| pubmed-article:911318 | pubmed:articleTitle | Bacterial catabolism of threonine. Threonine degradation initiated by L-threonine acetaldehyde-lyase (aldolase) in species of Pseudomonas. | lld:pubmed |
| pubmed-article:911318 | pubmed:publicationType | Journal Article | lld:pubmed |
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