| pubmed-article:8095409 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8095409 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:8095409 | lifeskim:mentions | umls-concept:C0007447 | lld:lifeskim |
| pubmed-article:8095409 | lifeskim:mentions | umls-concept:C0047421 | lld:lifeskim |
| pubmed-article:8095409 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:8095409 | lifeskim:mentions | umls-concept:C1523987 | lld:lifeskim |
| pubmed-article:8095409 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:8095409 | pubmed:dateCreated | 1993-4-13 | lld:pubmed |
| pubmed-article:8095409 | pubmed:abstractText | (S)-(3-Hydroxy-3-methyl-1-thionoglutaryl)-Coenzyme A (HMG[= S]CoA), a dithioester analog of (S)-(3-hydroxy-3-methylglutaryl)-CoA (HMG-CoA), acts as an efficient alternative substrate for avian HMG-CoA lyase. Detection of product formation by HPLC, UV absorbance and coupled enzyme assays indicates that HMG[= S]CoA cleavage yields acetyl[= S]CoA and acetoacetate. HMG[= S]CoA binds to the lyase with a Km of 13 microM and undergoes the cleavage reaction at a maximal rate which is 20% of that observed with HMG-CoA. The enzyme-catalyzed cleavage of both HMG-CoA and HMG[= S]CoA is stimulated by the divalent cations Mg2+ and Mn2+. Mg2+ produces a 2-fold higher stimulation of HMG-CoA cleavage than that observed with Mn2+. In contrast, stimulation of HMG[= S]CoA cleavage is nearly seven times higher with Mn2+ than with Mg2+. Not only is the stimulation of enzymatic activity dependent on the cation, but also the Km values for Mg2+ and Mn2+ are dependent upon the substrate used. In contrast, the Km values for HMG-CoA and HMG[= S]CoA are not markedly dependent on the identity of the divalent cation. These results are compatible with the initial formation of a binary enzyme-substrate complex prior to binding of the divalent cation to produce a catalytically active enzyme-substrate-metal ternary complex. | lld:pubmed |
| pubmed-article:8095409 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8095409 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8095409 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8095409 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8095409 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8095409 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8095409 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8095409 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8095409 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8095409 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8095409 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8095409 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8095409 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8095409 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:8095409 | pubmed:author | pubmed-author:MiziorkoH MHM | lld:pubmed |
| pubmed-article:8095409 | pubmed:author | pubmed-author:AndersonV EVE | lld:pubmed |
| pubmed-article:8095409 | pubmed:author | pubmed-author:HruzP WPW | lld:pubmed |
| pubmed-article:8095409 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8095409 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:8095409 | pubmed:volume | 1162 | lld:pubmed |
| pubmed-article:8095409 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8095409 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8095409 | pubmed:pagination | 149-54 | lld:pubmed |
| pubmed-article:8095409 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8095409 | pubmed:meshHeading | pubmed-meshheading:8095409-... | lld:pubmed |
| pubmed-article:8095409 | pubmed:meshHeading | pubmed-meshheading:8095409-... | lld:pubmed |
| pubmed-article:8095409 | pubmed:meshHeading | pubmed-meshheading:8095409-... | lld:pubmed |
| pubmed-article:8095409 | pubmed:meshHeading | pubmed-meshheading:8095409-... | lld:pubmed |
| pubmed-article:8095409 | pubmed:meshHeading | pubmed-meshheading:8095409-... | lld:pubmed |
| pubmed-article:8095409 | pubmed:meshHeading | pubmed-meshheading:8095409-... | lld:pubmed |
| pubmed-article:8095409 | pubmed:meshHeading | pubmed-meshheading:8095409-... | lld:pubmed |
| pubmed-article:8095409 | pubmed:meshHeading | pubmed-meshheading:8095409-... | lld:pubmed |
| pubmed-article:8095409 | pubmed:meshHeading | pubmed-meshheading:8095409-... | lld:pubmed |
| pubmed-article:8095409 | pubmed:meshHeading | pubmed-meshheading:8095409-... | lld:pubmed |
| pubmed-article:8095409 | pubmed:meshHeading | pubmed-meshheading:8095409-... | lld:pubmed |
| pubmed-article:8095409 | pubmed:meshHeading | pubmed-meshheading:8095409-... | lld:pubmed |
| pubmed-article:8095409 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8095409 | pubmed:articleTitle | 3-Hydroxy-3-methylglutaryldithio-CoA: utility of an alternative substrate in elucidation of a role for HMG-CoA lyase's cation activator. | lld:pubmed |
| pubmed-article:8095409 | pubmed:affiliation | Department of Biochemistry, Medical College of Wisconsin, Milwaukee 53226. | lld:pubmed |
| pubmed-article:8095409 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8095409 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8095409 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8095409 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
