| pubmed-article:8294474 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8294474 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:8294474 | lifeskim:mentions | umls-concept:C0039005 | lld:lifeskim |
| pubmed-article:8294474 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:8294474 | lifeskim:mentions | umls-concept:C0002003 | lld:lifeskim |
| pubmed-article:8294474 | lifeskim:mentions | umls-concept:C0003765 | lld:lifeskim |
| pubmed-article:8294474 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8294474 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:8294474 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:8294474 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
| pubmed-article:8294474 | lifeskim:mentions | umls-concept:C0205372 | lld:lifeskim |
| pubmed-article:8294474 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:8294474 | pubmed:dateCreated | 1994-2-25 | lld:pubmed |
| pubmed-article:8294474 | pubmed:abstractText | Reaction of pig muscle aldose reductase with phenylglyoxal resulted in the chemical modification of 2 arginine residues with accompanying loss of catalytic activity. The amino acid sequences of radioactive peptides resulting from the reaction of aldose reductase with [14C]phenylglyoxal followed by tryptic digestion and high performance liquid chromatography separation allowed identification of the modified arginine residues as R268 and R293. In the presence of the coenzyme NADP+, R268 is protected from modification by phenylglyoxal, while R293 becomes hyper-reactive. Phenylglyoxal modification of aldose reductase is slowed 3-fold by the presence of the coenzyme analog ADPRP; however, both arginines are still modified. These chemical modification results are in complete accord with the previously determined crystal structures of human and porcine aldose reductase complexed with NADPH, NADP+, and ADPRP. These structures indicate that R268 is located at the adenosine binding site, salt bridged to the 2'-phosphate group of NADP(H) and ADPRP. Arginine 293 is near the surface of the enzyme and is part of the C-terminal loop. In the apoenzyme or the ADPRP complex, R293 is partially protected by loop 7; upon binding NADP(H), loop 7 folds down over the coenzyme, thus exposing R293 to solvent. Our modification studies provide further evidence of the conformational change that occurs during the aldose reductase catalytic cycle. | lld:pubmed |
| pubmed-article:8294474 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8294474 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8294474 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8294474 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8294474 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8294474 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8294474 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8294474 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8294474 | pubmed:author | pubmed-author:FlynnT GTG | lld:pubmed |
| pubmed-article:8294474 | pubmed:author | pubmed-author:GreenN CNC | lld:pubmed |
| pubmed-article:8294474 | pubmed:author | pubmed-author:BorhaniD WDW | lld:pubmed |
| pubmed-article:8294474 | pubmed:author | pubmed-author:KubiseskiT... | lld:pubmed |
| pubmed-article:8294474 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8294474 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:8294474 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:8294474 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8294474 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8294474 | pubmed:pagination | 2183-8 | lld:pubmed |
| pubmed-article:8294474 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8294474 | pubmed:meshHeading | pubmed-meshheading:8294474-... | lld:pubmed |
| pubmed-article:8294474 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8294474 | pubmed:articleTitle | Studies on pig aldose reductase. Identification of an essential arginine in the primary and tertiary structure of the enzyme. | lld:pubmed |
| pubmed-article:8294474 | pubmed:affiliation | Department of Biochemistry, Queen's University, Kingston, Ontario, Canada. | lld:pubmed |
| pubmed-article:8294474 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8294474 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8294474 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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