5zol | pdb_00005zol
Crystal structure of a three sites mutantion of FSAA complexed with HA and product
Structural highlights
Function[FSAA_ECOLI] Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone (DHA) and D-glyceraldehyde 3-phosphate via an aldolization reaction. Can utilize several aldehydes as acceptor compounds in vitro, and hydroxyacetone (HA) or 1-hydroxy-butan-2-one as alternative donor substrate. Is also able to catalyze the direct stereoselective self-aldol addition of glycolaldehyde to furnish D-(-)-threose, and cross-aldol reactions of glycolaldehyde to other aldehyde acceptors. Is not able to cleave fructose, fructose 1-phosphate, glucose 6-phosphate, sedoheptulose 1,7-bisphosphate, xylulose 5-phosphate, ribulose 5-phosphate, and fructose 1,6-bisphosphate; cannot use dihydroxyacetone phosphate as donor compound nor D-glyceraldehyde as acceptor. Does not display transaldolase activity.[1] [HAMAP-Rule:MF_00496][2] [3] Publication Abstract from PubMedThe combinatorial modulation of inter- and intra-subunit interactions of decameric d-fructose-6-phosphate aldolase A (FSAA) generated a triple-site variant I31T/Q59T/I195Q FSAA with 27- to 278-fold improvement in activity towards target heteroaromatic aldehydes. X-ray crystallographic data and molecular dynamics simulations ascribed the enhanced activity to the pronounced flexibility of the interface region between subunits, the expanded substrate entrance and binding pocket, and enhanced proton transfer, unambiguously demonstrating the efficiency of this strategy for engineering multimeric enzymes. The engineering of decameric d-fructose-6-phosphate aldolase A by combinatorial modulation of inter- and intra-subunit interactions.,Yang X, Wu L, Li A, Ye L, Zhou J, Yu H Chem Commun (Camb). 2020 Jul 14;56(55):7561-7564. doi: 10.1039/d0cc02437f. Epub, 2020 Jun 10. PMID:32519699[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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