| pubmed-article:177283 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:177283 | lifeskim:mentions | umls-concept:C0596533 | lld:lifeskim |
| pubmed-article:177283 | lifeskim:mentions | umls-concept:C0062958 | lld:lifeskim |
| pubmed-article:177283 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:177283 | pubmed:dateCreated | 1976-7-6 | lld:pubmed |
| pubmed-article:177283 | pubmed:abstractText | Homoserine kinase was purified to apparent homogeneity from a derepressed strain of Escherichia coli K12, using standard fractionation techniques. It is a dimer (Mr = 60000) composed of apparently identical polypeptide chains (Mr = 29000). Its amino acid composition and N-terminal sequence have been determined. L-Threonine is a competitive inhibitor of the substrate L-homoserine; this inhibition is straighforward and shows no sign of co-operativity. Evidence is presented that homoserine and threonine bind to the same site of this non-allosteric enzyme. The binding of homoserine and threonine can also be studied by difference spectroscopy; the latter studies reveal an unexpected effect of magnesium ions, which might be the basis for the unusual high Mg2+ requirement for optimal enzyme reaction. | lld:pubmed |
| pubmed-article:177283 | pubmed:language | eng | lld:pubmed |
| pubmed-article:177283 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:177283 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:177283 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:177283 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:177283 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:177283 | pubmed:author | pubmed-author:WalkerJJ | lld:pubmed |
| pubmed-article:177283 | pubmed:author | pubmed-author:Truffa-BachiP... | lld:pubmed |
| pubmed-article:177283 | pubmed:author | pubmed-author:CohenG NGN | lld:pubmed |
| pubmed-article:177283 | pubmed:author | pubmed-author:BurrBB | lld:pubmed |
| pubmed-article:177283 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:177283 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:177283 | pubmed:volume | 62 | lld:pubmed |
| pubmed-article:177283 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:177283 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:177283 | pubmed:pagination | 519-26 | lld:pubmed |
| pubmed-article:177283 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
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| pubmed-article:177283 | pubmed:year | 1976 | lld:pubmed |
| pubmed-article:177283 | pubmed:articleTitle | Homoserine kinase from Escherichia coli K12. | lld:pubmed |
| pubmed-article:177283 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:947498 | entrezgene:pubmed | pubmed-article:177283 | lld:entrezgene |
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