Targeted Mutation of a Non-catalytic Gating Residue Increases the Rate of Pseudomonas aeruginosa d-Arginine Dehydrogenase Catalytic Turnover.

ABSTRACT: Commercial food and l-amino acid industries rely on bioengineered d-amino acid oxidizing enzymes to detect and remove d-amino acid contaminants. However, the bioengineering of enzymes to generate faster biological catalysts has proven difficult as a result of the failure to target specific kinetic steps that limit enzyme turnover, k_cat, and the poor understanding of loop dynamics critical for catalysis. Pseudomonas aeruginosa d-arginine dehydrogenase (PaDADH) oxidizes most d-amino acids and is a good candidate for application in the l-amino acid and food industries. The side chain of the loop L2 E²⁴⁶ residue located at the entrance of the PaDADH active site pocket potentially favors the closed active site conformation and secures the substr

SUBMITTER: Quaye JA 

PROVIDER: S-EPMC10655190 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature