title: Structure-guided redesign of D-fructose-6-phosphate aldolase from E. coli: remarkable activity and selectivity towards acceptor substrates by two-point mutation.
abstract: Structure-guided re-design of the acceptor binding site of D-fructose-6-phosphate aldolase from E. coli leads to the construction of FSA A129S/A165G double mutant with an activity between 5- to >900-fold higher than that of wild-type towards N-Cbz-aminoaldehyde derivatives.
authors.affiliation: Instituto de Química Avanzada de Cataluña-CSIC, Jordi Girona 18-26, 08034 Barcelona, Spain.
authors.forename: Mariana
authors.initials: M
authors.lastname: Gutierrez
authors.forename: Teodor
authors.initials: T
authors.lastname: Parella
authors.forename: Jesús
authors.initials: J
authors.lastname: Joglar
authors.forename: Jordi
authors.initials: J
authors.lastname: Bujons
authors.forename: Pere
authors.initials: P
authors.lastname: Clapés
mesh_terms: D000446:Aldehyde-Lyases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D019943:Amino Acid Substitution; D001665:Binding Sites; D020134:Catalytic Domain; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017354:Point Mutation; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
chemical_list: D029968:Escherichia coli Proteins; D000446:Aldehyde-Lyases; C426024:fsaA protein, E coli