Disease relevance of L-fuculose

• Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure [1].

High impact information on L-fuculose

• Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis [2].
• In general, when fucO becomes constitutively expressed, two other simultaneous changes occur: the fucA gene encoding fuculose-1-phosphate aldolase becomes constitutively expressed and the fucPIK operon encoding fucose permease, fucose isomerase, and fuculose kinase becomes noninducible [3].
• The positive regulator encoded by fucR responds to fuculose 1-phosphate as the effector [4].
• All of these mutants had enzyme patterns similar to that of strain 3; namely, fucose permease, fucose isomerase, and fuculose kinase were noninducible, whereas fuculose 1-phosphate aldolase was constitutive [5].

References