| pubmed-article:2996505 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2996505 | lifeskim:mentions | umls-concept:C0031659 | lld:lifeskim |
| pubmed-article:2996505 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:2996505 | lifeskim:mentions | umls-concept:C0679932 | lld:lifeskim |
| pubmed-article:2996505 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
| pubmed-article:2996505 | lifeskim:mentions | umls-concept:C0047701 | lld:lifeskim |
| pubmed-article:2996505 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2996505 | pubmed:dateCreated | 1985-11-21 | lld:pubmed |
| pubmed-article:2996505 | pubmed:abstractText | The phosphonomethyl analogue of 3-phosphoglycerate (2-hydroxy-4-phosphonobutanoate) is a potent competitive inhibitor of cofactor-dependent phosphoglycerate mutase from yeast and of cofactor-independent phosphoglycerate mutase from wheat germ. For the yeast enzyme Ki is 1.3 mM (Km for substrate is 0.71 mM); for the wheatgerm enzyme Ki is 18 mM (Km for substrate is 0.86 mM). This analogue should be a useful tool for n.m.r. spectroscopic studies on the mechanism of action of the two mutases. The arsonomethyl analogue of 3-phosphoglycerate (4-arsono-2-hydroxybutanoate) was a relatively poor inhibitor. | lld:pubmed |
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| pubmed-article:2996505 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2996505 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2996505 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2996505 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2996505 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:2996505 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:2996505 | pubmed:author | pubmed-author:DixonH BHB | lld:pubmed |
| pubmed-article:2996505 | pubmed:author | pubmed-author:Fothergill-Gi... | lld:pubmed |
| pubmed-article:2996505 | pubmed:author | pubmed-author:McAleeseS MSM | lld:pubmed |
| pubmed-article:2996505 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2996505 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2996505 | pubmed:volume | 230 | lld:pubmed |
| pubmed-article:2996505 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2996505 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2996505 | pubmed:pagination | 535-42 | lld:pubmed |
| pubmed-article:2996505 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:2996505 | pubmed:meshHeading | pubmed-meshheading:2996505-... | lld:pubmed |
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| pubmed-article:2996505 | pubmed:meshHeading | pubmed-meshheading:2996505-... | lld:pubmed |
| pubmed-article:2996505 | pubmed:meshHeading | pubmed-meshheading:2996505-... | lld:pubmed |
| pubmed-article:2996505 | pubmed:meshHeading | pubmed-meshheading:2996505-... | lld:pubmed |
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| pubmed-article:2996505 | pubmed:meshHeading | pubmed-meshheading:2996505-... | lld:pubmed |
| pubmed-article:2996505 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:2996505 | pubmed:articleTitle | The phosphonomethyl analogue of 3-phosphoglycerate is a potent competitive inhibitor of phosphoglycerate mutases. | lld:pubmed |
| pubmed-article:2996505 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2996505 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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