| pubmed-article:10832099 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10832099 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10832099 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:10832099 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:10832099 | lifeskim:mentions | umls-concept:C1413917 | lld:lifeskim |
| pubmed-article:10832099 | lifeskim:mentions | umls-concept:C0443199 | lld:lifeskim |
| pubmed-article:10832099 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:10832099 | pubmed:issue | 2-3 | lld:pubmed |
| pubmed-article:10832099 | pubmed:dateCreated | 2000-8-9 | lld:pubmed |
| pubmed-article:10832099 | pubmed:abstractText | Both enzymatic and autocatalytic mechanisms have been proposed to account for protein thioacylation (commonly known as palmitoylation). Acyl-CoA binding proteins (ACBP) strongly suppress non-enzymatic thioacylation of cysteinyl-containing peptides by long-chain acyl-CoAs. At physiological concentrations of ACBP, acyl-CoAs, and membrane lipids, the rate of spontaneous acylation is expected to be too slow to contribute significantly to thioacylation of signaling proteins in mammalian cells (Leventis et al., Biochemistry 36 (1997) 5546-5553). Here we characterized the effects of ACBP on enzymatic thioacylation. A protein S-acyltransferase activity previously characterized using G-protein alpha-subunits as a substrate (Dunphy et al., J. Biol. Chem., 271 (1996) 7154-7159), was capable of thioacylating short lipid-modified cysteinyl-containing peptides. The minimum requirements for substrate recognition were a free cysteine thiol adjacent to a hydrophobic lipid anchor, either myristate or farnesyl isoprenoid. PAT activity displayed specificity for the acyl donor, efficiently utilizing long-chain acyl-CoAs, but not free fatty acid or S-palmitoyl-N-acetylcysteamine. ACBP only modestly inhibited enzymatic thioacylation of a myristoylated peptide or G-protein alpha-subunits under conditions where non-enzymatic thioacylation was reduced to background. Thus, protein S-acyltransferase remains active in the presence of physiological concentrations of ACBP and acyl-CoA in vitro and is likely to represent the predominant mechanism of thioacylation in vivo. | lld:pubmed |
| pubmed-article:10832099 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10832099 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10832099 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10832099 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10832099 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10832099 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10832099 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10832099 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10832099 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10832099 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10832099 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10832099 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10832099 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10832099 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10832099 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10832099 | pubmed:month | May | lld:pubmed |
| pubmed-article:10832099 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:10832099 | pubmed:author | pubmed-author:SchroederHH | lld:pubmed |
| pubmed-article:10832099 | pubmed:author | pubmed-author:SilviusJ RJR | lld:pubmed |
| pubmed-article:10832099 | pubmed:author | pubmed-author:LinderM EME | lld:pubmed |
| pubmed-article:10832099 | pubmed:author | pubmed-author:LeventisRR | lld:pubmed |
| pubmed-article:10832099 | pubmed:author | pubmed-author:DunphyJ TJT | lld:pubmed |
| pubmed-article:10832099 | pubmed:author | pubmed-author:GreentreeW... | lld:pubmed |
| pubmed-article:10832099 | pubmed:author | pubmed-author:KnudsenJ KJK | lld:pubmed |
| pubmed-article:10832099 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10832099 | pubmed:day | 31 | lld:pubmed |
| pubmed-article:10832099 | pubmed:volume | 1485 | lld:pubmed |
| pubmed-article:10832099 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10832099 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10832099 | pubmed:pagination | 185-98 | lld:pubmed |
| pubmed-article:10832099 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:10832099 | pubmed:meshHeading | pubmed-meshheading:10832099... | lld:pubmed |
| pubmed-article:10832099 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10832099 | pubmed:articleTitle | Differential effects of acyl-CoA binding protein on enzymatic and non-enzymatic thioacylation of protein and peptide substrates. | lld:pubmed |
| pubmed-article:10832099 | pubmed:affiliation | Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110, USA. | lld:pubmed |
| pubmed-article:10832099 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10832099 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10832099 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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