Human farnesyl pyrophosphate synthase is allosterically inhibited by its own product
Farnesyl pyrophosphate (FPP) is a key building block for the synthesis of many lipids. Here the authors determine the crystal structure of farnesyl pyrophosphate synthase (FPPS) with its bound product and use kinetic measurements to show that FPP is an allosteric effector of the enzyme.
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Nature Portfolio
2017
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oai:doaj.org-article:111b9b63900a4b0cbd2922f6e12767282021-12-02T14:42:40ZHuman farnesyl pyrophosphate synthase is allosterically inhibited by its own product10.1038/ncomms141322041-1723https://doaj.org/article/111b9b63900a4b0cbd2922f6e12767282017-01-01T00:00:00Zhttps://doi.org/10.1038/ncomms14132https://doaj.org/toc/2041-1723Farnesyl pyrophosphate (FPP) is a key building block for the synthesis of many lipids. Here the authors determine the crystal structure of farnesyl pyrophosphate synthase (FPPS) with its bound product and use kinetic measurements to show that FPP is an allosteric effector of the enzyme.Jaeok ParkMichal ZielinskiAlexandr MagderYoula S. TsantrizosAlbert M. BerghuisNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-8 (2017) |
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Science Q Jaeok Park Michal Zielinski Alexandr Magder Youla S. Tsantrizos Albert M. Berghuis Human farnesyl pyrophosphate synthase is allosterically inhibited by its own product |
description |
Farnesyl pyrophosphate (FPP) is a key building block for the synthesis of many lipids. Here the authors determine the crystal structure of farnesyl pyrophosphate synthase (FPPS) with its bound product and use kinetic measurements to show that FPP is an allosteric effector of the enzyme. |
format |
article |
author |
Jaeok Park Michal Zielinski Alexandr Magder Youla S. Tsantrizos Albert M. Berghuis |
author_facet |
Jaeok Park Michal Zielinski Alexandr Magder Youla S. Tsantrizos Albert M. Berghuis |
author_sort |
Jaeok Park |
title |
Human farnesyl pyrophosphate synthase is allosterically inhibited by its own product |
title_short |
Human farnesyl pyrophosphate synthase is allosterically inhibited by its own product |
title_full |
Human farnesyl pyrophosphate synthase is allosterically inhibited by its own product |
title_fullStr |
Human farnesyl pyrophosphate synthase is allosterically inhibited by its own product |
title_full_unstemmed |
Human farnesyl pyrophosphate synthase is allosterically inhibited by its own product |
title_sort |
human farnesyl pyrophosphate synthase is allosterically inhibited by its own product |
publisher |
Nature Portfolio |
publishDate |
2017 |
url |
https://doaj.org/article/111b9b63900a4b0cbd2922f6e1276728 |
work_keys_str_mv |
AT jaeokpark humanfarnesylpyrophosphatesynthaseisallostericallyinhibitedbyitsownproduct AT michalzielinski humanfarnesylpyrophosphatesynthaseisallostericallyinhibitedbyitsownproduct AT alexandrmagder humanfarnesylpyrophosphatesynthaseisallostericallyinhibitedbyitsownproduct AT youlastsantrizos humanfarnesylpyrophosphatesynthaseisallostericallyinhibitedbyitsownproduct AT albertmberghuis humanfarnesylpyrophosphatesynthaseisallostericallyinhibitedbyitsownproduct |
_version_ |
1718389612668256256 |