| pubmed-article:2879558 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2879558 | lifeskim:mentions | umls-concept:C0001022 | lld:lifeskim |
| pubmed-article:2879558 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:2879558 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:2879558 | pubmed:dateCreated | 1987-2-27 | lld:pubmed |
| pubmed-article:2879558 | pubmed:abstractText | Because of certain similarities between acetyl-CoA carboxylase (ACC) and tubulin, and the recent demonstration of the ADP-ribosylation of tubulin by cholera toxin, we have investigated a potential role for ADP-ribosylation in the regulation of ACC activity. Incubation of purified rat liver ACC with cholera toxin in the presence of millimolar concentrations of [adenylate-32P]NAD results in a time-dependent incorporation of ADP-ribose into ACC of greater than 2 mol/mol of enzyme subunit, accompanied by a marked inactivation of enzyme activity. This effect is not mimicked by pertussis toxin, ADP-ribose, or ribose 5-phosphate. Incubation of labeled ACC with snake venom phosphodiesterase and alkaline hydrolysis release 32P-products tentatively identified by high-performance liquid chromatography as 5'-[32P]AMP and [32P]ADP-ribose, respectively. These data are consistent with a mono-ADP-ribosylation of ACC catalyzed by cholera toxin. Phosphodiesterase treatment of inactivated ACC partially restores enzyme activity. The effects of ADP-ribosylation of ACC are expressed both as a decrease in the enzyme Vmax and as an increase in the apparent Ka for citrate. These results suggest that ACC might be a substrate for endogenous ADP-ribosyltransferases and that this covalent modification could be an important regulatory mechanism for the modulation of fatty acid synthesis in vivo. | lld:pubmed |
| pubmed-article:2879558 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2879558 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2879558 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2879558 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2879558 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2879558 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2879558 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2879558 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2879558 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2879558 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2879558 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2879558 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2879558 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2879558 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:2879558 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:2879558 | pubmed:author | pubmed-author:WittersL ALA | lld:pubmed |
| pubmed-article:2879558 | pubmed:author | pubmed-author:McDermottJ... | lld:pubmed |
| pubmed-article:2879558 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2879558 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:2879558 | pubmed:volume | 25 | lld:pubmed |
| pubmed-article:2879558 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2879558 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2879558 | pubmed:pagination | 7216-20 | lld:pubmed |
| pubmed-article:2879558 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:2879558 | pubmed:meshHeading | pubmed-meshheading:2879558-... | lld:pubmed |
| pubmed-article:2879558 | pubmed:meshHeading | pubmed-meshheading:2879558-... | lld:pubmed |
| pubmed-article:2879558 | pubmed:meshHeading | pubmed-meshheading:2879558-... | lld:pubmed |
| pubmed-article:2879558 | pubmed:meshHeading | pubmed-meshheading:2879558-... | lld:pubmed |
| pubmed-article:2879558 | pubmed:meshHeading | pubmed-meshheading:2879558-... | lld:pubmed |
| pubmed-article:2879558 | pubmed:meshHeading | pubmed-meshheading:2879558-... | lld:pubmed |
| pubmed-article:2879558 | pubmed:meshHeading | pubmed-meshheading:2879558-... | lld:pubmed |
| pubmed-article:2879558 | pubmed:meshHeading | pubmed-meshheading:2879558-... | lld:pubmed |
| pubmed-article:2879558 | pubmed:meshHeading | pubmed-meshheading:2879558-... | lld:pubmed |
| pubmed-article:2879558 | pubmed:meshHeading | pubmed-meshheading:2879558-... | lld:pubmed |
| pubmed-article:2879558 | pubmed:meshHeading | pubmed-meshheading:2879558-... | lld:pubmed |
| pubmed-article:2879558 | pubmed:meshHeading | pubmed-meshheading:2879558-... | lld:pubmed |
| pubmed-article:2879558 | pubmed:meshHeading | pubmed-meshheading:2879558-... | lld:pubmed |
| pubmed-article:2879558 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:2879558 | pubmed:articleTitle | Regulation of acetyl-CoA carboxylase by ADP-ribosylation. | lld:pubmed |
| pubmed-article:2879558 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2879558 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
