3tu9
From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ALDOA_RABIT ALDOA_RABIT]] Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.<ref>PMID:17329259</ref> | [[http://www.uniprot.org/uniprot/ALDOA_RABIT ALDOA_RABIT]] Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.<ref>PMID:17329259</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Several 5-O-alkyl- and 5-C-alkyl-mannitol bis-phosphates were synthesized and comparatively assayed as inhibitors of fructose bis-phosphate aldolases (Fbas) from rabbit muscle (taken as surrogate model of the human enzyme) and from Trypanosoma brucei. A limited selectivity was found in several instances. Crystallographic studies confirm that the 5-O-methyl derivative binds competitively with substrate and the 5-O-methyl moiety penetrating deeper into a shallow hydrophobic pocket at the active site. This observation can lead to the preparation of selective competitive or irreversible inhibitors of the parasite Fba. | ||
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| + | Mannitol Bis-phosphate Based Inhibitors of Fructose 1,6-Bisphosphate Aldolases.,Mabiala-Bassiloua CG, Arthus-Cartier G, Hannaert V, Therisod H, Sygusch J, Therisod M ACS Med Chem Lett. 2011 Sep 3;2(11):804-8. doi: 10.1021/ml200129s. eCollection, 2011 Nov 10. PMID:24900268<ref>PMID:24900268</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3tu9" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Revision as of 06:06, 18 April 2018
Crystal structure of rabbit muscle aldolase bound with 5-O-methyl mannitol 1,6-phosphate
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