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| pubmed-article:8198521 | lifeskim:mentions | umls-concept:C0079870 | lld:lifeskim |
| pubmed-article:8198521 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:8198521 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:8198521 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:8198521 | lifeskim:mentions | umls-concept:C0026845 | lld:lifeskim |
| pubmed-article:8198521 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8198521 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8198521 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8198521 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8198521 | pubmed:dateCreated | 1994-6-28 | lld:pubmed |
| pubmed-article:8198521 | pubmed:abstractText | Asp-130 of the recombinant skeletal-muscle 6-phosphofructo-2-kinase (PFK-2)/fructose-2,6-bisphosphatase was mutated into Ala in order to study its role in catalysis and/or substrate binding. The D130A mutant displayed a 30- to 140-fold decreased 2-kinase Vmax, depending on the pH, and a 30- and 60-fold increase in Km for MgATP and Fru-6-P respectively at pH 8.5 compared with the wild-type. Mutagenesis of Asp-130 to Ala had no effect on the 2-phosphatase activity, and fluorescence measurements indicated that the changes in kinetic properties of PFK-2 in the D130A mutant were not due to instability. The role of Asp-130 in the 2-kinase reaction is discussed and compared with that of Asp-103 of 6-phosphofructo-1-kinase from Escherichia coli, which binds Mg2+. | lld:pubmed |
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| pubmed-article:8198521 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8198521 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8198521 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8198521 | pubmed:month | May | lld:pubmed |
| pubmed-article:8198521 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:8198521 | pubmed:author | pubmed-author:HueLL | lld:pubmed |
| pubmed-article:8198521 | pubmed:author | pubmed-author:BertrandLL | lld:pubmed |
| pubmed-article:8198521 | pubmed:author | pubmed-author:RiderM HMH | lld:pubmed |
| pubmed-article:8198521 | pubmed:author | pubmed-author:CrepinK MKM | lld:pubmed |
| pubmed-article:8198521 | pubmed:author | pubmed-author:De CloedtMM | lld:pubmed |
| pubmed-article:8198521 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8198521 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8198521 | pubmed:volume | 300 ( Pt 1) | lld:pubmed |
| pubmed-article:8198521 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8198521 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8198521 | pubmed:pagination | 111-5 | lld:pubmed |
| pubmed-article:8198521 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8198521 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8198521 | pubmed:articleTitle | Site-directed mutagenesis of rat muscle 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: role of Asp-130 in the 2-kinase domain. | lld:pubmed |
| pubmed-article:8198521 | pubmed:affiliation | Hormone and Metabolic Research Unit, International Institute of Cellular and Molecular Pathology, Brussels, Belgium. | lld:pubmed |
| pubmed-article:8198521 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8198521 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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