The enzyme L-fuculose-phosphate aldolase (EC 4.1.2.17) catalyzes the chemical reaction
L-fuculose-1-phosphate ⇌ {\displaystyle \rightleftharpoons } glycerone phosphate + (S)-lactaldehyde This enzyme belongs to the family of lyases, specifically the aldehyde-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-fuculose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming). Other names in common use include L-fuculose 1-phosphate aldolase, fuculose aldolase, and L-fuculose-1-phosphate lactaldehyde-lyase. This enzyme participates in fructose and mannose metabolism.
Structural studies As of late 2007, 20 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1DZU, PDB: 1DZV, PDB: 1DZW, PDB: 1DZX, PDB: 1DZY, PDB: 1DZZ, PDB: 1E46, PDB: 1E47, PDB: 1E48, PDB: 1E49, PDB: 1E4A, PDB: 1E4B, PDB: 1E4C, PDB: 1FUA, PDB: 2FK5, PDB: 2FLF, PDB: 2FUA, PDB: 2OPI, PDB: 3FUA, and PDB: 4FUA.
See also Fuculose L-Fuculose kinase
References
Ghalambor MA, Heath EC (1966). "The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. IV. Purification and properties of cytidine monophosphate 3-deoxy-d-manno-octulosonate synthetase". J. Biol. Chem. 241 (13): 3216–21. doi:10.1016/S0021-9258(18)96517-8. PMID 5330266. Dreyer MK, Schulz GE (1993). "The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli". J. Mol. Biol. 231 (3): 549–53. doi:10.1006/jmbi.1993.1307. PMID 8515438. Dreyer MK, Schulz GE (1996). "Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure". J. Mol. Biol. 259 (3): 458–66. doi:10.1006/jmbi.1996.0332. PMID 8676381.
