Redesign of MST enzymes to target lyase activity instead promotes mutase and dehydratase activities.

ABSTRACT: The isochorismate and salicylate synthases are members of the MST family of enzymes. The isochorismate synthases establish an equilibrium for the conversion chorismate to isochorismate and the reverse reaction. The salicylate synthases convert chorismate to salicylate with an isochorismate intermediate; therefore, the salicylate synthases perform isochorismate synthase and isochorismate-pyruvate lyase activities sequentially. While the active site residues are highly conserved, there are two sites that show trends for lyase-activity and lyase-deficiency. Using steady state kinetics and HPLC progress curves, we tested the "interchange" hypothesis that interconversion of the amino acids at these sites would promote lyase activity in the isochorismate synthases and remove lyase activity from

SUBMITTER: Meneely KM 

PROVIDER: S-EPMC3836504 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature