The effect of ligands on the thermal stability of sulfotransferases: a molecular dynamics simulation study
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| 008 | 210128e20150401xx s 000 0 eng | ||
| 024 | 7 | 0 | |a 10.1007/s00894-015-2625-1 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00894-015-2625-1 | ||
| 245 | 0 | 4 | |a The effect of ligands on the thermal stability of sulfotransferases: a molecular dynamics simulation study |h [Elektronische Daten] |c [Pu-pu Zhang, Li Zhao, Shi-yang Long, Pu Tian] |
| 520 | 3 | |a Human cytosolic sulfotransferases (hSULTs) are important phase II metabolic enzymes. They catalyze transfer of the sulfuryl-group (-SO3) from 3′-phosphoadenosine 5′-phosphosulfate (PAPS) to the hydroxyl or primary amine moieties of a large number of endogenous and xenobiotic substrates. Broad selectivity and specificity of binding and activity within the sulfortransferases family could be detected by thermal denaturation assays, which have been made more and more suitable for high throughput screening based on recent technical advances. Here molecular dynamics simulations were used to explore the effect of the cofactor (PAPS) and substrate (LCA) on the thermal stability of the enzyme. It was found that the apo-enzyme unfolded fastest upon heating. The holo-enzyme with bound substrate LCA unfolded slowest. This thermo-denaturation order is consistent with that observed in experiments. Further it was found that the cofactor and substrate will pronouncedly increase the thermal stability of the active pocket regions that interact directly with the ligands. In addition, cofactor and substrate show noticeable synergy effect on the thermal stability of the enzyme. Graphical Abstract Human cytosolic sulfotransferase 2A1 | |
| 540 | |a Springer-Verlag Berlin Heidelberg, 2015 | ||
| 690 | 7 | |a Human cytosolic sulfotransferase 2A1 |2 nationallicence | |
| 690 | 7 | |a Molecular dynamic simulations |2 nationallicence | |
| 690 | 7 | |a Thermal stability |2 nationallicence | |
| 700 | 1 | |a Zhang |D Pu-pu |u School of Life Sciences, Jilin University, Changchun, China |4 aut | |
| 700 | 1 | |a Zhao |D Li |u School of Life Sciences, Jilin University, Changchun, China |4 aut | |
| 700 | 1 | |a Long |D Shi-yang |u School of Life Sciences, Jilin University, Changchun, China |4 aut | |
| 700 | 1 | |a Tian |D Pu |u School of Life Sciences, Jilin University, Changchun, China |4 aut | |
| 773 | 0 | |t Journal of Molecular Modeling |d Springer Berlin Heidelberg |g 21/4(2015-04-01), 1-7 |x 1610-2940 |q 21:4<1 |1 2015 |2 21 |o 894 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00894-015-2625-1 |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a research-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00894-015-2625-1 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Zhang |D Pu-pu |u School of Life Sciences, Jilin University, Changchun, China |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Zhao |D Li |u School of Life Sciences, Jilin University, Changchun, China |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Long |D Shi-yang |u School of Life Sciences, Jilin University, Changchun, China |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Tian |D Pu |u School of Life Sciences, Jilin University, Changchun, China |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Journal of Molecular Modeling |d Springer Berlin Heidelberg |g 21/4(2015-04-01), 1-7 |x 1610-2940 |q 21:4<1 |1 2015 |2 21 |o 894 | ||