L-fuculose-1-phosphate lactaldehyde-lyase
GLU 73;HIS 92;HIS 94;HIS 155(Zinc binding)
The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli.
Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli.
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND CATALYTIC MECHANISM.
Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure.
Epimerization via carbon-carbon bond cleavage. L-ribulose-5-phosphate 4-epimerase as a masked class II aldolase.
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS), AND MUTAGENESIS.
Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis.
13C and deuterium isotope effects suggest an aldol cleavage mechanism for L-ribulose-5-phosphate 4-epimerase.
Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis.
The structure of L-ribulose-5-phosphate 4-epimerase: an aldolase-like platform for epimerization.
Catalysis and binding in L-ribulose-5-phosphate 4-epimerase: a comparison with L-fuculose-1-phosphate aldolase.
This enzyme belongs to the aldolase class II family, which utilizes the metal ion as cofactor.