| pubmed-article:39 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:39 | lifeskim:mentions | umls-concept:C0017786 | lld:lifeskim |
| pubmed-article:39 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:39 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:39 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:39 | lifeskim:mentions | umls-concept:C0205374 | lld:lifeskim |
| pubmed-article:39 | pubmed:issue | 23 | lld:pubmed |
| pubmed-article:39 | pubmed:dateCreated | 1976-2-19 | lld:pubmed |
| pubmed-article:39 | pubmed:abstractText | The reaction of glutamate dehydrogenase and glutamate (gl) with NAD+ and NADP+ has been studied with stopped-flow techniques. The enzyme was in all experiments present in excess of the coenzyme. The results indicate that the ternary complex (E-NAD(P)H-kg) is present as an intermediate in the formation of the stable complex (E-NAD(P)H-gl). The identification of the complexes is based on their absorption spectra. The binding of the coenzyme to (E-gl) is the rate-limiting step in the formation of (E-NAD(P)H-kg) while the dissociation of alpha-ketoglutarate (kg) from this complex is the rate-limiting step in the formation of (E-NAD(P)H-gl). The Km for glutamate was 20-25 mM in the first reaction and 3 mM in the formation of the stable complex. The Km values were independent of the coenzyme. The reaction rates with NAD+ were approximately 50% greater than those with NADP+. Furthermore, high glutamate concentration inhibited the formation of (E-NADH-kg) while no substrate inhibition was found with NADP+ as coenzyme. ADP enhanced while GTP reduced the rate of (E-NAD(P)H-gl) formation. The rate of formation of (E-NAD(P)H-kg) was inhibited by ADP, while it increased at high glutamate concentration when small amounts of GTP were added. The results show that the higher activity found with NAD+ compared to NADP+ under steady-state assay conditions do not necessarily involve binding of NAD+ to the ADP activating site of the enzyme. Moreover, the substrate inhibition found at high glutamate concentration under steady-state assay condition is not due to the formation of (E-NAD(P)H-gl) as this complex is formed with Km of 3 mM glutamate, and the substrate inhibition is only significant at 20-30 times this concentration. | lld:pubmed |
| pubmed-article:39 | pubmed:language | eng | lld:pubmed |
| pubmed-article:39 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:39 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:39 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:39 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:39 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:39 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:39 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:39 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:39 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:39 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:39 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:39 | pubmed:author | pubmed-author:SannerTT | lld:pubmed |
| pubmed-article:39 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:39 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:39 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:39 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:39 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:39 | pubmed:pagination | 5094-8 | lld:pubmed |
| pubmed-article:39 | pubmed:dateRevised | 2003-11-14 | lld:pubmed |
| pubmed-article:39 | pubmed:meshHeading | pubmed-meshheading:39-Anima... | lld:pubmed |
| pubmed-article:39 | pubmed:meshHeading | pubmed-meshheading:39-Liver | lld:pubmed |
| pubmed-article:39 | pubmed:meshHeading | pubmed-meshheading:39-Cattl... | lld:pubmed |
| pubmed-article:39 | pubmed:meshHeading | pubmed-meshheading:39-Kinet... | lld:pubmed |
| pubmed-article:39 | pubmed:meshHeading | pubmed-meshheading:39-Gluta... | lld:pubmed |
| pubmed-article:39 | pubmed:meshHeading | pubmed-meshheading:39-NAD | lld:pubmed |
| pubmed-article:39 | pubmed:meshHeading | pubmed-meshheading:39-Time... | lld:pubmed |
| pubmed-article:39 | pubmed:meshHeading | pubmed-meshheading:39-NADP | lld:pubmed |
| pubmed-article:39 | pubmed:meshHeading | pubmed-meshheading:39-Prote... | lld:pubmed |
| pubmed-article:39 | pubmed:meshHeading | pubmed-meshheading:39-Gluta... | lld:pubmed |
| pubmed-article:39 | pubmed:meshHeading | pubmed-meshheading:39-Bindi... | lld:pubmed |
| pubmed-article:39 | pubmed:meshHeading | pubmed-meshheading:39-Guano... | lld:pubmed |
| pubmed-article:39 | pubmed:meshHeading | pubmed-meshheading:39-Adeno... | lld:pubmed |
| pubmed-article:39 | pubmed:meshHeading | pubmed-meshheading:39-Spect... | lld:pubmed |
| pubmed-article:39 | pubmed:year | 1975 | lld:pubmed |
| pubmed-article:39 | pubmed:articleTitle | Formation of transient complexes in the glutamate dehydrogenase catalyzed reaction. | lld:pubmed |
| pubmed-article:39 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:39 | lld:pubmed |
