Different Sensitivities of Mutants and ChimericForms of Human Muscle and Liver Fructose-1,6-Bisphosphatases towards AMP
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| 024 | 7 | 0 | |a 10.1515/BC.2003.006 |2 doi |
| 035 | |a (NATIONALLICENCE)gruyter-10.1515/BC.2003.006 | ||
| 245 | 0 | 0 | |a Different Sensitivities of Mutants and ChimericForms of Human Muscle and Liver Fructose-1,6-Bisphosphatases towards AMP |h [Elektronische Daten] |c [D. Rakus, H. Tillmann, R. Wysocki, S. Ulaszewski, K. Eschrich, A. Dzugaj] |
| 520 | 3 | |a AMP is an allosteric inhibitor of human muscle and liver fructose-1,6-bisphosphatase (FBPase). Despite strong similarity of the nucleotide binding domains, the muscle enzyme is inhibited by AMP approximately 35 times stronger than liver FBPase: I0.5 for muscle and for liver FBPase are 0.14 uM and 4.8 uM, respectively. Chimeric human muscle (L50M288) and chimeric human liver enzymes (M50L288), in which the N-terminal residues (1-50) were derived from the human liver and human muscle FBPases, respectively, were inhibited by AMP 2-3 times stronger than the wild-type liver enzyme. An amino acid exchange within the Nterminal region of the muscle enzyme towards liver FBPase (Lys20→Glu) resulted in 13-fold increased I0.5 values compared to the wild-type muscle enzyme. However, the opposite exchanges in the liver enzyme (Glu20→Lys and double mutation Glu19→Asp/Glu20→Lys) did not change the sensitivity for AMP inhibition of the liver mutant (I0.5 value of 4.9 uM). The decrease of sensitivity for AMP of the muscle mutant Lys20→Glu, as well as the lack of changes in the inhibition by AMP of liver mutants Glu20→Lys and Glu19→Asp/Glu20→Lys, suggest a different mechanism of AMP binding to the muscle and liver enzyme. | |
| 540 | |a Copyright © 2003 by Walter de Gruyter GmbH & Co. KG | ||
| 690 | 7 | |a Biochemistry |2 nationallicence | |
| 690 | 7 | |a Molecular biology |2 nationallicence | |
| 690 | 7 | |a Cellular biology |2 nationallicence | |
| 700 | 1 | |a Rakus |D D. |4 aut | |
| 700 | 1 | |a Tillmann |D H. |4 aut | |
| 700 | 1 | |a Wysocki |D R. |4 aut | |
| 700 | 1 | |a Ulaszewski |D S. |4 aut | |
| 700 | 1 | |a Eschrich |D K. |4 aut | |
| 700 | 1 | |a Dzugaj |D A. |4 aut | |
| 773 | 0 | |t Biological Chemistry |d Walter de Gruyter |g 384/1(2003-01-27), 51-58 |x 1431-6730 |q 384:1<51 |1 2003 |2 384 |o bchm | |
| 856 | 4 | 0 | |u https://doi.org/10.1515/BC.2003.006 |q text/html |z Onlinezugriff via DOI |
| 908 | |D 1 |a research article |2 jats | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1515/BC.2003.006 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Rakus |D D. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Tillmann |D H. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Wysocki |D R. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Ulaszewski |D S. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Eschrich |D K. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Dzugaj |D A. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Biological Chemistry |d Walter de Gruyter |g 384/1(2003-01-27), 51-58 |x 1431-6730 |q 384:1<51 |1 2003 |2 384 |o bchm | ||
| 900 | 7 | |b CC0 |u http://creativecommons.org/publicdomain/zero/1.0 |2 nationallicence | |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-gruyter | ||