Structural highlights
Function
[ALDOA_RABIT] Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.[1]
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ St-Jean M, Izard T, Sygusch J. A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with Wiskott-Aldrich syndrome protein. J Biol Chem. 2007 May 11;282(19):14309-15. Epub 2007 Feb 27. PMID:17329259 doi:10.1074/jbc.M611505200
- ↑ Mabiala-Bassiloua CG, Arthus-Cartier G, Hannaert V, Therisod H, Sygusch J, Therisod M. Mannitol Bis-phosphate Based Inhibitors of Fructose 1,6-Bisphosphate Aldolases. ACS Med Chem Lett. 2011 Sep 3;2(11):804-8. doi: 10.1021/ml200129s. eCollection, 2011 Nov 10. PMID:24900268 doi:http://dx.doi.org/10.1021/ml200129s
