| pubmed-article:2310379 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2310379 | lifeskim:mentions | umls-concept:C0034342 | lld:lifeskim |
| pubmed-article:2310379 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:2310379 | pubmed:dateCreated | 1990-4-9 | lld:pubmed |
| pubmed-article:2310379 | pubmed:abstractText | Pyruvate decarboxylase from Zymomonas mobilis is inhibited by 3-hydroxypyruvate, which can also act as a poor substrate. While catalysing the decarboxylation of this alternative substrate, the enzyme undergoes a progressive but partial inactivation over several hours. The extent of inactivation depends upon the pH and upon the concentration of 3-hydroxypyruvate. After partial inactivation and removal of unchanged 3-hydroxypyruvate, enzymic activity recovers slowly. We suggest that inactivation results from accumulation of enzyme-bound glycollaldehyde, which is relatively stable, possibly because it is dehydrated to form an acetyl group. | lld:pubmed |
| pubmed-article:2310379 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2310379 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2310379 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2310379 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2310379 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2310379 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2310379 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2310379 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2310379 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2310379 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2310379 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2310379 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2310379 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2310379 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2310379 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2310379 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2310379 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:2310379 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:2310379 | pubmed:author | pubmed-author:DugglebyR GRG | lld:pubmed |
| pubmed-article:2310379 | pubmed:author | pubmed-author:ThomasGG | lld:pubmed |
| pubmed-article:2310379 | pubmed:author | pubmed-author:DiefenbachRR | lld:pubmed |
| pubmed-article:2310379 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2310379 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2310379 | pubmed:volume | 266 | lld:pubmed |
| pubmed-article:2310379 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2310379 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2310379 | pubmed:pagination | 305-8 | lld:pubmed |
| pubmed-article:2310379 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:2310379 | pubmed:meshHeading | pubmed-meshheading:2310379-... | lld:pubmed |
| pubmed-article:2310379 | pubmed:meshHeading | pubmed-meshheading:2310379-... | lld:pubmed |
| pubmed-article:2310379 | pubmed:meshHeading | pubmed-meshheading:2310379-... | lld:pubmed |
| pubmed-article:2310379 | pubmed:meshHeading | pubmed-meshheading:2310379-... | lld:pubmed |
| pubmed-article:2310379 | pubmed:meshHeading | pubmed-meshheading:2310379-... | lld:pubmed |
| pubmed-article:2310379 | pubmed:meshHeading | pubmed-meshheading:2310379-... | lld:pubmed |
| pubmed-article:2310379 | pubmed:meshHeading | pubmed-meshheading:2310379-... | lld:pubmed |
| pubmed-article:2310379 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2310379 | pubmed:articleTitle | Inactivation of pyruvate decarboxylase by 3-hydroxypyruvate. | lld:pubmed |
| pubmed-article:2310379 | pubmed:affiliation | Department of Biochemistry, University of Queensland, St. Lucia, Australia. | lld:pubmed |
| pubmed-article:2310379 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2310379 | pubmed:publicationType | Comparative Study | lld:pubmed |
