| pubmed-article:1304341 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1304341 | lifeskim:mentions | umls-concept:C0317708 | lld:lifeskim |
| pubmed-article:1304341 | lifeskim:mentions | umls-concept:C0030016 | lld:lifeskim |
| pubmed-article:1304341 | lifeskim:mentions | umls-concept:C0017725 | lld:lifeskim |
| pubmed-article:1304341 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:1304341 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:1304341 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:1304341 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:1304341 | pubmed:dateCreated | 1993-7-6 | lld:pubmed |
| pubmed-article:1304341 | pubmed:abstractText | Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase (G6PD) was isolated in high yield and purified to homogeneity from a newly constructed strain of Escherichia coli which lacks its own glucose 6-phosphate dehydrogenase gene. Lys-21 is one of two lysyl residues in the enzyme previously modified by the affinity labels pyridoxal 5'-phosphate and pyridoxal 5'-diphosphate-5'-adenosine, which are competitive inhibitors of the enzyme with respect to glucose 6-phosphate (LaDine, J.R., Carlow, D., Lee, W.T., Cross, R.L., Flynn, T.G., & Levy, H.R., 1991, J. Biol. Chem. 266, 5558-5562). K21R and K21Q mutants of the enzyme were purified to homogeneity and characterized kinetically to determine the function of Lys-21. Both mutant enzymes showed increased Km-values for glucose 6-phosphate compared to wild-type enzyme: 1.4-fold (NAD-linked reaction) and 2.1-fold (NADP-linked reaction) for the K21R enzyme, and 36-fold (NAD-linked reaction) and 53-fold (NADP-linked reaction) for the K21Q enzyme. The Km for NADP+ was unchanged in both mutant enzymes. The Km for NAD+ was increased 1.5- and 3.2-fold, compared to the wild-type enzyme, in the K21R and K21Q enzymes, respectively. For the K21R enzyme the kcat for the NAD- and NADP-linked reactions was unchanged. The kcat for the K21Q enzyme was increased in the NAD-linked reaction by 26% and decreased by 30% in the NADP-linked reaction from the values for the wild-type enzyme. The data are consistent with Lys-21 participating in the binding of the phosphate group of the substrate to the enzyme via charge-charge interaction. | lld:pubmed |
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| pubmed-article:1304341 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1304341 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1304341 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1304341 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1304341 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1304341 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:1304341 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:1304341 | pubmed:author | pubmed-author:LeviH BHB | lld:pubmed |
| pubmed-article:1304341 | pubmed:author | pubmed-author:LeeW TWT | lld:pubmed |
| pubmed-article:1304341 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1304341 | pubmed:volume | 1 | lld:pubmed |
| pubmed-article:1304341 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1304341 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1304341 | pubmed:pagination | 329-34 | lld:pubmed |
| pubmed-article:1304341 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
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| pubmed-article:1304341 | pubmed:meshHeading | pubmed-meshheading:1304341-... | lld:pubmed |
| pubmed-article:1304341 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1304341 | pubmed:articleTitle | Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding through charge-charge interaction. | lld:pubmed |
| pubmed-article:1304341 | pubmed:affiliation | Department of Biology, Syracuse University, New York 13244-1220. | lld:pubmed |
| pubmed-article:1304341 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1304341 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:1304341 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1304341 | lld:pubmed |
