Overview for MACiE Entry M0072
EC Number: 126.96.36.199 (A member of the Lyases, Carbon-carbon lyases, Aldehyde-lyases)
Enzyme Name: L-fuculose-phosphate aldolase
Biological Species: Escherichia coli (Bacteria)
Catalytic Chain UniprotKB Accession Codes:
- P0AB87 - L-fuculose phosphate aldolase
Representative PDB Code: 1fua - L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T (Resolution = 1.92 Å).
Catalytic CATH Codes:
Display structure information
Overall Comment: Dreyer et al. claim that Tyr113' is the main catalytic residue involved. However pKa studies and a Y113F mutant suggest that Glu73 is more likely .
View similar reactions
Stepwise Description of the Reaction
|Step 1||Ring opening of the sugar occurs outside of the enzyme active site.|
|Step 2||Glu73 deprotonates the substrate alcohol at the C4 position, resulting in the elimination of the ene-diolate intermediate and the formation of the product lactaldehyde.|
|Step 3||The ene-diolate intermediate deprotonates Glu73.|
View similar reactions (composite manual annotation)
Catalytic Residues Involved
||Location of Function
Metal Cofactors for M0072
- A. C. Joerger et al. (2000), Biochemistry, 39, 6033-6041. Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis.
- M. K. Dreyer et al. (1996), J. Mol. Biol., 259, 458-466. Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure.
Homologue information for M0072 (1fua)
MACiE Homologues (within the PDB)
MACiE Homologues (within UniprotKB/SwissProt)
Entries with at least one Catalytic CATH code in common (different mechanisms):
|M0273 ||L-ribulose-5-phosphate 4-epimerase |
Links to this entry in other databases