Structural highlights
Function
[ALDOA_RABIT] Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of fructose 1,6-bisphosphate aldolase shows three distinct modes of product binding that are correlated to the disposition of the C-terminal region and depicts a possible trajectory for product exchange. The structure also indicates binding preference for monobasic triose phosphates.
Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase.,Blom N, Sygusch J Nat Struct Biol. 1997 Jan;4(1):36-9. PMID:8989320[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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
- ↑ Blom N, Sygusch J. Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase. Nat Struct Biol. 1997 Jan;4(1):36-9. PMID:8989320
