Structural highlights
5zol is a 10 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 2.172Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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 PubMed
The 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.
See Also
References
- ↑ Schurmann M, Sprenger GA. Fructose-6-phosphate aldolase is a novel class I aldolase from Escherichia coli and is related to a novel group of bacterial transaldolases. J Biol Chem. 2001 Apr 6;276(14):11055-61. Epub 2000 Dec 18. PMID:11120740 doi:http://dx.doi.org/10.1074/jbc.M008061200
- ↑ Sugiyama M, Hong Z, Liang PH, Dean SM, Whalen LJ, Greenberg WA, Wong CH. D-Fructose-6-phosphate aldolase-catalyzed one-pot synthesis of iminocyclitols. J Am Chem Soc. 2007 Nov 28;129(47):14811-7. Epub 2007 Nov 7. PMID:17985886 doi:http://dx.doi.org/10.1021/ja073911i
- ↑ Garrabou X, Castillo JA, Guerard-Helaine C, Parella T, Joglar J, Lemaire M, Clapes P. Asymmetric self- and cross-aldol reactions of glycolaldehyde catalyzed by D-fructose-6-phosphate aldolase. Angew Chem Int Ed Engl. 2009;48(30):5521-5. doi: 10.1002/anie.200902065. PMID:19554584 doi:http://dx.doi.org/10.1002/anie.200902065
- ↑ Yang X, Wu L, Li A, Ye L, Zhou J, Yu H. The engineering of decameric d-fructose-6-phosphate aldolase A by combinatorial modulation of inter- and intra-subunit interactions. Chem Commun (Camb). 2020 Jul 14;56(55):7561-7564. doi: 10.1039/d0cc02437f. Epub, 2020 Jun 10. PMID:32519699 doi:http://dx.doi.org/10.1039/d0cc02437f
