| pubmed-article:4030785 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:4030785 | lifeskim:mentions | umls-concept:C0038592 | lld:lifeskim |
| pubmed-article:4030785 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:4030785 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:4030785 | pubmed:dateCreated | 1985-10-11 | lld:pubmed |
| pubmed-article:4030785 | pubmed:abstractText | L-myo-Inositol-1-phosphate synthase has been found to have at least a 5-fold preference for the beta-anomer of its natural substrate D-Glc-6-P. The alpha-anomer appears to be an inhibitor of the reaction and may be converted to product as well. As well as showing an enzymatic preference for the equatorial C-1 hydroxyl of D-Glc-6-P, our results suggest that it is the pyranose form of D-Glc-6-P that binds to the enzyme and that ring-opening is an enzymatic step. We have also found D-2-dGlc-6-P, D-2-F-2-dGlc-6-P, and D-Man-6-P each to be both competitive inhibitors and substrates that are converted to inositol phosphates by the synthase. D-Allose-6-P is a weak inhibitor of the enzyme, but not a substrate. D-Gal-6-P is neither substrate nor inhibitor. Thus the specificity of the synthase with respect to single position epimers of D-Glc-6-P increases in the order C1 less than C2 much less than C3 less than C4. | lld:pubmed |
| pubmed-article:4030785 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4030785 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4030785 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4030785 | pubmed:language | eng | lld:pubmed |
| pubmed-article:4030785 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4030785 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:4030785 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4030785 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4030785 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4030785 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:4030785 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:4030785 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:4030785 | pubmed:author | pubmed-author:ShermanW RWR | lld:pubmed |
| pubmed-article:4030785 | pubmed:author | pubmed-author:WongY HYH | lld:pubmed |
| pubmed-article:4030785 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:4030785 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:4030785 | pubmed:volume | 260 | lld:pubmed |
| pubmed-article:4030785 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:4030785 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:4030785 | pubmed:pagination | 11083-90 | lld:pubmed |
| pubmed-article:4030785 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:4030785 | pubmed:meshHeading | pubmed-meshheading:4030785-... | lld:pubmed |
| pubmed-article:4030785 | pubmed:meshHeading | pubmed-meshheading:4030785-... | lld:pubmed |
| pubmed-article:4030785 | pubmed:meshHeading | pubmed-meshheading:4030785-... | lld:pubmed |
| pubmed-article:4030785 | pubmed:meshHeading | pubmed-meshheading:4030785-... | lld:pubmed |
| pubmed-article:4030785 | pubmed:meshHeading | pubmed-meshheading:4030785-... | lld:pubmed |
| pubmed-article:4030785 | pubmed:meshHeading | pubmed-meshheading:4030785-... | lld:pubmed |
| pubmed-article:4030785 | pubmed:meshHeading | pubmed-meshheading:4030785-... | lld:pubmed |
| pubmed-article:4030785 | pubmed:meshHeading | pubmed-meshheading:4030785-... | lld:pubmed |
| pubmed-article:4030785 | pubmed:meshHeading | pubmed-meshheading:4030785-... | lld:pubmed |
| pubmed-article:4030785 | pubmed:meshHeading | pubmed-meshheading:4030785-... | lld:pubmed |
| pubmed-article:4030785 | pubmed:meshHeading | pubmed-meshheading:4030785-... | lld:pubmed |
| pubmed-article:4030785 | pubmed:meshHeading | pubmed-meshheading:4030785-... | lld:pubmed |
| pubmed-article:4030785 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:4030785 | pubmed:articleTitle | Anomeric and other substrate specificity studies with myo-inositol-1-P synthase. | lld:pubmed |
| pubmed-article:4030785 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:4030785 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4030785 | lld:pubmed |
