| pubmed-article:3902830 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3902830 | lifeskim:mentions | umls-concept:C0030946 | lld:lifeskim |
| pubmed-article:3902830 | lifeskim:mentions | umls-concept:C0034351 | lld:lifeskim |
| pubmed-article:3902830 | lifeskim:mentions | umls-concept:C0391871 | lld:lifeskim |
| pubmed-article:3902830 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:3902830 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:3902830 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:3902830 | pubmed:dateCreated | 1985-12-13 | lld:pubmed |
| pubmed-article:3902830 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3902830 | pubmed:abstractText | The pyruvate oxidase of Escherichia coli is a homo-tetrameric enzyme which can be activated greater than 500-fold (kcat/Km) by limited proteolytic digestion with alpha-chymotrypsin in the presence of pyruvate and thiamine pyrophosphate. The cleavage produces an Mr 2000 peptide (the alpha-peptide) from each subunit and mimics the physiologically important activation of the enzyme by phospholipids. Moreover, the proteolytic cleavage results in the loss of the high affinity lipid-binding site of the enzyme. We now report the isolation and characterization of the alpha-peptide fragment which is cleaved from the carboxyl terminus of each subunit by protease activation. Both the site of cleavage and the sequence of the alpha-peptide have been determined by a combination of Edman degradation of the purified peptide and DNA sequence analysis of the gene encoding the oxidase. The cleavage site lies within a sequence of hydrophobic amino acids predicted to form a beta-sheet. Another segment of the alpha-peptide is predicted to form an amphipathic alpha-helix. Quantitative assessment of the amphipathic nature of this alpha-helix (Eisenberg, D. (1984) Annu. Rev. Biochem. 53, 595-623) gives a value very similar to the values for several helical peptides which spontaneously bind to the surface of phospholipid vesicles. From these analyses, we propose that the alpha-peptide may play a role in binding pyruvate oxidase to cell membrane phospholipids in vivo. | lld:pubmed |
| pubmed-article:3902830 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3902830 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3902830 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3902830 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3902830 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3902830 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3902830 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3902830 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3902830 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3902830 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3902830 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3902830 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:3902830 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:3902830 | pubmed:author | pubmed-author:HagerL PLP | lld:pubmed |
| pubmed-article:3902830 | pubmed:author | pubmed-author:CronanJ EJEJr | lld:pubmed |
| pubmed-article:3902830 | pubmed:author | pubmed-author:RecnyM AMA | lld:pubmed |
| pubmed-article:3902830 | pubmed:author | pubmed-author:GrabauCC | lld:pubmed |
| pubmed-article:3902830 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3902830 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:3902830 | pubmed:volume | 260 | lld:pubmed |
| pubmed-article:3902830 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3902830 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3902830 | pubmed:pagination | 14287-91 | lld:pubmed |
| pubmed-article:3902830 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:3902830 | pubmed:meshHeading | pubmed-meshheading:3902830-... | lld:pubmed |
| pubmed-article:3902830 | pubmed:meshHeading | pubmed-meshheading:3902830-... | lld:pubmed |
| pubmed-article:3902830 | pubmed:meshHeading | pubmed-meshheading:3902830-... | lld:pubmed |
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| pubmed-article:3902830 | pubmed:meshHeading | pubmed-meshheading:3902830-... | lld:pubmed |
| pubmed-article:3902830 | pubmed:meshHeading | pubmed-meshheading:3902830-... | lld:pubmed |
| pubmed-article:3902830 | pubmed:meshHeading | pubmed-meshheading:3902830-... | lld:pubmed |
| pubmed-article:3902830 | pubmed:meshHeading | pubmed-meshheading:3902830-... | lld:pubmed |
| pubmed-article:3902830 | pubmed:meshHeading | pubmed-meshheading:3902830-... | lld:pubmed |
| pubmed-article:3902830 | pubmed:meshHeading | pubmed-meshheading:3902830-... | lld:pubmed |
| pubmed-article:3902830 | pubmed:meshHeading | pubmed-meshheading:3902830-... | lld:pubmed |
| pubmed-article:3902830 | pubmed:meshHeading | pubmed-meshheading:3902830-... | lld:pubmed |
| pubmed-article:3902830 | pubmed:meshHeading | pubmed-meshheading:3902830-... | lld:pubmed |
| pubmed-article:3902830 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:3902830 | pubmed:articleTitle | Characterization of the alpha-peptide released upon protease activation of pyruvate oxidase. | lld:pubmed |
| pubmed-article:3902830 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3902830 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3902830 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| entrez-gene:946132 | entrezgene:pubmed | pubmed-article:3902830 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:3902830 | lld:entrezgene |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3902830 | lld:pubmed |
