| pubmed-article:1101964 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1101964 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1101964 | lifeskim:mentions | umls-concept:C0034342 | lld:lifeskim |
| pubmed-article:1101964 | lifeskim:mentions | umls-concept:C0039848 | lld:lifeskim |
| pubmed-article:1101964 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:1101964 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:1101964 | lifeskim:mentions | umls-concept:C0443288 | lld:lifeskim |
| pubmed-article:1101964 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:1101964 | lifeskim:mentions | umls-concept:C1261552 | lld:lifeskim |
| pubmed-article:1101964 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1101964 | pubmed:dateCreated | 1976-1-8 | lld:pubmed |
| pubmed-article:1101964 | pubmed:abstractText | Pyruvate decarboxylase dissociates into sub-units of one half the molecular weight at alkaline pH. At the same conditions the cofactors thiamine pyrophosphate and Mg2+ are released and can be separated from the protein. Thiamine pyrophosphate is an obligatory cofactor for reconstitution to the oligomer [1]. In this study the effect of thiamine pyrophosphate derivatives (thiamine monophosphate, thiamine, and thiazole pyrophosphate) upon the reconstitution procedure was evaluated. The complete association of sub-units to form active oligomer was attained only when thiamine pyrophosphate was present. It is concluded that both the pyrimidine ring and the pyrophosphate group are required for productive co-enzyme binding and it is proposed that this interaction effects a conformational change which promotes protomer aggregation to form the enzymatically active holoenzyme. In addition data are presented which indicate that the monomer unit is 60 000 +/- 3000 daltons and that the N-terminal amino acid is histidine. Since the molecular weight of the active oligomer is 230 000 it is proposed that pyruvate decarboxylase is a tetramer comprised of four identical or nearly identical monomer units. | lld:pubmed |
| pubmed-article:1101964 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1101964 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1101964 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1101964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1101964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1101964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1101964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1101964 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1101964 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1101964 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:1101964 | pubmed:author | pubmed-author:GounarisA DAD | lld:pubmed |
| pubmed-article:1101964 | pubmed:author | pubmed-author:TurkenkopfII | lld:pubmed |
| pubmed-article:1101964 | pubmed:author | pubmed-author:CiverchiaL... | lld:pubmed |
| pubmed-article:1101964 | pubmed:author | pubmed-author:GreenlieJJ | lld:pubmed |
| pubmed-article:1101964 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1101964 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:1101964 | pubmed:volume | 405 | lld:pubmed |
| pubmed-article:1101964 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1101964 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1101964 | pubmed:pagination | 492-9 | lld:pubmed |
| pubmed-article:1101964 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1101964 | pubmed:meshHeading | pubmed-meshheading:1101964-... | lld:pubmed |
| pubmed-article:1101964 | pubmed:meshHeading | pubmed-meshheading:1101964-... | lld:pubmed |
| pubmed-article:1101964 | pubmed:meshHeading | pubmed-meshheading:1101964-... | lld:pubmed |
| pubmed-article:1101964 | pubmed:meshHeading | pubmed-meshheading:1101964-... | lld:pubmed |
| pubmed-article:1101964 | pubmed:meshHeading | pubmed-meshheading:1101964-... | lld:pubmed |
| pubmed-article:1101964 | pubmed:meshHeading | pubmed-meshheading:1101964-... | lld:pubmed |
| pubmed-article:1101964 | pubmed:meshHeading | pubmed-meshheading:1101964-... | lld:pubmed |
| pubmed-article:1101964 | pubmed:meshHeading | pubmed-meshheading:1101964-... | lld:pubmed |
| pubmed-article:1101964 | pubmed:year | 1975 | lld:pubmed |
| pubmed-article:1101964 | pubmed:articleTitle | Pyruvate decarboxylase III. Specificity restrictions for thiamine pyrophosphate in the protein association step, sub-unit structure. | lld:pubmed |
| pubmed-article:1101964 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1101964 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1101964 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1101964 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1101964 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1101964 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1101964 | lld:pubmed |
