pubmed-article:12123640 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12123640 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
pubmed-article:12123640 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:12123640 | lifeskim:mentions | umls-concept:C0035331 | lld:lifeskim |
pubmed-article:12123640 | lifeskim:mentions | umls-concept:C1417746 | lld:lifeskim |
pubmed-article:12123640 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:12123640 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:12123640 | pubmed:dateCreated | 2002-7-18 | lld:pubmed |
pubmed-article:12123640 | pubmed:abstractText | Protein myristoylation occurs when the 14 carbon fatty acid, myristic acid, is covalently attached by amide linkage to a protein's N -terminal glycine by an N -terminal myristoyltransferase (NMT). A variation of this called heterogeneous acylation occurs in vivo only in retina when specific proteins are modified by myristic acid (14:0), tetradecenoic acid (14:1 n-9), tetradecadienoic acid (14:2n -6), and lauric acid (12:0). Myristic and lauric acids are relatively rare, comprising approximately 1% of the fatty acids in the retina. The unsaturated fatty acids 14:1 n-9 and 14:2 n-6 are less abundant, but can be synthesized in retina by retroconversion of 18:1 n-9 and 18:2 n-6 fatty acids, respectively. A previous quantitative study of acyl-CoA pools in bovine retina, heart, and liver found comparable levels of acyl-CoAs in each tissue, indicating that heterogeneous acylation is not due to limiting amounts of myristoyl-CoA in retina. In this current study the authors have characterized a panel of purified recombinant Type I and II NMTs found in retina and liver by assessing their utilization of the four acyl-CoAs used in vivo to acylate retina proteins. Acceptor peptides used in these assays were derived from the N -termini of src which is only myristoylated in vivo, and the cAMP dependent kinase A catalytic subunit which is heterogeneously acylated in retina, but myristoylated in other tissues. The authors have tested the ability of unlabelled acyl-CoAs to compete with [(3)H] myristoyl-CoA transfer, the efficacy of an NMT inhibitory protein (NIP(71)), and acyl-CoA affinity chromatography was used to isolate endogenous NMT inhibitory factor(s) from bovine heart and retina tissue homogenates. These results provide a basis of kinetic parameters and enzymatic characterization for Type I and Type II NMTs with two acceptor peptides and the four physiologically relevant fatty acid-CoAs found on retinal proteins, but do not indicate that heterogeneous acylation is a specialized function of any of the enzymes tested in this study. | lld:pubmed |
pubmed-article:12123640 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12123640 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12123640 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12123640 | pubmed:language | eng | lld:pubmed |
pubmed-article:12123640 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12123640 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12123640 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12123640 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12123640 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12123640 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12123640 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12123640 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12123640 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12123640 | pubmed:month | Jul | lld:pubmed |
pubmed-article:12123640 | pubmed:issn | 0014-4835 | lld:pubmed |
pubmed-article:12123640 | pubmed:author | pubmed-author:RajalaRaju... | lld:pubmed |
pubmed-article:12123640 | pubmed:author | pubmed-author:AndersonRober... | lld:pubmed |
pubmed-article:12123640 | pubmed:author | pubmed-author:RundleDana... | lld:pubmed |
pubmed-article:12123640 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12123640 | pubmed:volume | 75 | lld:pubmed |
pubmed-article:12123640 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12123640 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12123640 | pubmed:pagination | 87-97 | lld:pubmed |
pubmed-article:12123640 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:12123640 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:12123640 | pubmed:articleTitle | Characterization of Type I and Type II myristoyl-CoA:protein N-myristoyltransferases with the Acyl-CoAs found on heterogeneously acylated retinal proteins. | lld:pubmed |
pubmed-article:12123640 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, U.S.A. | lld:pubmed |
pubmed-article:12123640 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12123640 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:12123640 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12123640 | lld:pubmed |