| pubmed-article:7578040 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7578040 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:7578040 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:7578040 | lifeskim:mentions | umls-concept:C0002003 | lld:lifeskim |
| pubmed-article:7578040 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:7578040 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:7578040 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:7578040 | lifeskim:mentions | umls-concept:C0439831 | lld:lifeskim |
| pubmed-article:7578040 | pubmed:issue | 44 | lld:pubmed |
| pubmed-article:7578040 | pubmed:dateCreated | 1995-12-18 | lld:pubmed |
| pubmed-article:7578040 | pubmed:abstractText | Transient kinetic data for D-xylose reduction with NADPH and NADPD and for xylitol oxidation with NADP+ catalyzed by recombinant C298A mutant human aldose reductase at pH 8 have been used to obtain estimates for each of the rate constants in the complete reaction mechanism as outlined for the wild-type enzyme in the preceding paper (Grimshaw et al., 1995a). Analysis of the resulting kinetic model shows that the nearly 9-fold increase in Vxylose/Et for C298A mutant enzyme relative to wild-type human aldose reductase is due entirely to an 8.7-fold increase in the rate constant for the conformational change that converts the tight (Ki NADP+ = 0.14 microM) binary *E.NADP+ complex to the weak (Kd NADP+ = 6.8 microM) E.NADP+ complex from which NADP+ is released. Evaluation of the rate expressions derived from the kinetic model for the various steady-state kinetic parameters reveals that the 37-fold increase in Kxylose seen for C298A relative to wild-type aldose reductase is largely due to this same increase in the net rate of NADP+ release; the rate constant for xylose binding accounts for only a factor of 5.5. A similar 17-fold increase in the rate constant for the conformational change preceding NADPH release does not, however, result in any increase in Vxylitol/Et, because hydride transfer is largely rate-limiting for reaction in this direction.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
| pubmed-article:7578040 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7578040 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7578040 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7578040 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7578040 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7578040 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7578040 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7578040 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7578040 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7578040 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:7578040 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:7578040 | pubmed:author | pubmed-author:GrimshawC ECE | lld:pubmed |
| pubmed-article:7578040 | pubmed:author | pubmed-author:LaiC JCJ | lld:pubmed |
| pubmed-article:7578040 | pubmed:author | pubmed-author:GabbayK HKH | lld:pubmed |
| pubmed-article:7578040 | pubmed:author | pubmed-author:BohrenK MKM | lld:pubmed |
| pubmed-article:7578040 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7578040 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:7578040 | pubmed:volume | 34 | lld:pubmed |
| pubmed-article:7578040 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7578040 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7578040 | pubmed:pagination | 14366-73 | lld:pubmed |
| pubmed-article:7578040 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:7578040 | pubmed:meshHeading | pubmed-meshheading:7578040-... | lld:pubmed |
| pubmed-article:7578040 | pubmed:meshHeading | pubmed-meshheading:7578040-... | lld:pubmed |
| pubmed-article:7578040 | pubmed:meshHeading | pubmed-meshheading:7578040-... | lld:pubmed |
| pubmed-article:7578040 | pubmed:meshHeading | pubmed-meshheading:7578040-... | lld:pubmed |
| pubmed-article:7578040 | pubmed:meshHeading | pubmed-meshheading:7578040-... | lld:pubmed |
| pubmed-article:7578040 | pubmed:meshHeading | pubmed-meshheading:7578040-... | lld:pubmed |
| pubmed-article:7578040 | pubmed:meshHeading | pubmed-meshheading:7578040-... | lld:pubmed |
| pubmed-article:7578040 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7578040 | pubmed:articleTitle | Human aldose reductase: subtle effects revealed by rapid kinetic studies of the C298A mutant enzyme. | lld:pubmed |
| pubmed-article:7578040 | pubmed:affiliation | Whittier Diabetes Program, Department of Medicine, University of California, San Diego, La Jolla 92093-0983, USA. | lld:pubmed |
| pubmed-article:7578040 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7578040 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7578040 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7578040 | lld:pubmed |
