pubmed-article:1244119 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1244119 | lifeskim:mentions | umls-concept:C0599840 | lld:lifeskim |
pubmed-article:1244119 | lifeskim:mentions | umls-concept:C0009235 | lld:lifeskim |
pubmed-article:1244119 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:1244119 | lifeskim:mentions | umls-concept:C0064448 | lld:lifeskim |
pubmed-article:1244119 | lifeskim:mentions | umls-concept:C0597599 | lld:lifeskim |
pubmed-article:1244119 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:1244119 | pubmed:issue | 1-6 | lld:pubmed |
pubmed-article:1244119 | pubmed:dateCreated | 1978-3-10 | lld:pubmed |
pubmed-article:1244119 | pubmed:abstractText | Kynureninase was purified to homogeneity from the extracts of Pseudomonas marginalis and Neurospora crassa. The active kynureninase containing pyridoxal 5'-phosphate transaminates with L-ornithine or L-alanine to form the inactive pyridoxamine 5'-phosphate form of enzyme and delta1-pyrroline-2-carboxylate or pyruvate. This inactive enzyme transaminates with pyruvate to restore the active pyridoxal 5'-phosphate enzyme and L-alanine. The activity of kynureninase is regulated in this manner by transamination of the coenzyme moiety. | lld:pubmed |
pubmed-article:1244119 | pubmed:language | eng | lld:pubmed |
pubmed-article:1244119 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1244119 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1244119 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1244119 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1244119 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1244119 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1244119 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1244119 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1244119 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1244119 | pubmed:issn | 0300-8924 | lld:pubmed |
pubmed-article:1244119 | pubmed:author | pubmed-author:SodaKK | lld:pubmed |
pubmed-article:1244119 | pubmed:author | pubmed-author:TanizawaKK | lld:pubmed |
pubmed-article:1244119 | pubmed:author | pubmed-author:MoriguchiMM | lld:pubmed |
pubmed-article:1244119 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1244119 | pubmed:volume | 29 | lld:pubmed |
pubmed-article:1244119 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1244119 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1244119 | pubmed:pagination | 335-8 | lld:pubmed |
pubmed-article:1244119 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:1244119 | pubmed:meshHeading | pubmed-meshheading:1244119-... | lld:pubmed |
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pubmed-article:1244119 | pubmed:meshHeading | pubmed-meshheading:1244119-... | lld:pubmed |
pubmed-article:1244119 | pubmed:meshHeading | pubmed-meshheading:1244119-... | lld:pubmed |
pubmed-article:1244119 | pubmed:meshHeading | pubmed-meshheading:1244119-... | lld:pubmed |
pubmed-article:1244119 | pubmed:meshHeading | pubmed-meshheading:1244119-... | lld:pubmed |
pubmed-article:1244119 | pubmed:year | 1975 | lld:pubmed |
pubmed-article:1244119 | pubmed:articleTitle | Regulation of the activity of microbial kynureninase by transamination of the enzyme-bound coenzyme. | lld:pubmed |
pubmed-article:1244119 | pubmed:publicationType | Journal Article | lld:pubmed |