| pubmed-article:2492527 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2492527 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2492527 | lifeskim:mentions | umls-concept:C0085221 | lld:lifeskim |
| pubmed-article:2492527 | lifeskim:mentions | umls-concept:C0002003 | lld:lifeskim |
| pubmed-article:2492527 | lifeskim:mentions | umls-concept:C0024337 | lld:lifeskim |
| pubmed-article:2492527 | lifeskim:mentions | umls-concept:C0034266 | lld:lifeskim |
| pubmed-article:2492527 | lifeskim:mentions | umls-concept:C0205681 | lld:lifeskim |
| pubmed-article:2492527 | lifeskim:mentions | umls-concept:C0178463 | lld:lifeskim |
| pubmed-article:2492527 | lifeskim:mentions | umls-concept:C0072697 | lld:lifeskim |
| pubmed-article:2492527 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:2492527 | pubmed:dateCreated | 1989-3-21 | lld:pubmed |
| pubmed-article:2492527 | pubmed:abstractText | The reaction of aldose reductase from human psoas muscle with either pyridoxal 5'-phosphate (PLP) or pyridoxal 5'-diphospho-5'-adenosine (PLP-AMP) results in a pseudo first-order 2-fold activation of the enzyme with the stoichiometric incorporation of 1 mol of either reagent per mol of enzyme. However, in addition to an increase in Vmax there was also an increase in Km for both substrate, DL-glyceraldehyde, and coenzyme, NADPH. This resulted in an overall decrease in catalytic efficiency (kcat/Km). Spectral analysis indicated that activation by both PLP and PLP-AMP was accompanied by Schiff's base formation and epsilon-pyridoxyllysine was identified in hydrolysates of the reduced enzyme PLP-complex. Digestion of either PLP-modified or PLP-AMP-modified aldose reductase with endoproteinase Lys-C followed by high performance liquid chromatography purification and amino acid sequencing of the pyridoxyllated peptide revealed that PLP and PLP-AMP had modified the same lysine residue. A 32-residue peptide containing the essential lysine was found to be highly homologous with a segment of the sequence of both human liver aldehyde reductase and rat lens aldose reductase. A tetrapeptide (Ile-Pro-Lys-Ser) containing the essential lysine was identical in all three enzymes. These results highlight the close structural similarity between members of the aldehyde reductase family. | lld:pubmed |
| pubmed-article:2492527 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2492527 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2492527 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2492527 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2492527 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2492527 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:2492527 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:2492527 | pubmed:author | pubmed-author:FlynnT GTG | lld:pubmed |
| pubmed-article:2492527 | pubmed:author | pubmed-author:LyonsCC | lld:pubmed |
| pubmed-article:2492527 | pubmed:author | pubmed-author:MorjanaN ANA | lld:pubmed |
| pubmed-article:2492527 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2492527 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2492527 | pubmed:volume | 264 | lld:pubmed |
| pubmed-article:2492527 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2492527 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2492527 | pubmed:pagination | 2912-9 | lld:pubmed |
| pubmed-article:2492527 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:2492527 | pubmed:meshHeading | pubmed-meshheading:2492527-... | lld:pubmed |
| pubmed-article:2492527 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2492527 | pubmed:articleTitle | Aldose reductase from human psoas muscle. Affinity labeling of an active site lysine by pyridoxal 5'-phosphate and pyridoxal 5'-diphospho-5'-adenosine. | lld:pubmed |
| pubmed-article:2492527 | pubmed:affiliation | Department of Biochemistry, Queen's University, Kingston, Ontario, Canada. | lld:pubmed |
| pubmed-article:2492527 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2492527 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:231 | entrezgene:pubmed | pubmed-article:2492527 | lld:entrezgene |
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