Probing remote residues important for catalysis in Escherichia coli ornithine transcarbamoylase.

ABSTRACT: Understanding how enzymes achieve their tremendous catalytic power is a major question in biochemistry. Greater understanding is also needed for enzyme engineering applications. In many cases, enzyme efficiency and specificity depend on residues not in direct contact with the substrate, termed remote residues. This work focuses on Escherichia coli ornithine transcarbamoylase (OTC), which plays a central role in amino acid metabolism. OTC has been reported to undergo an induced-fit conformational change upon binding its first substrate, carbamoyl phosphate (CP), and several residues important for activity have been identified. Using computational methods based on the computed chemical properties from theoretical titration curves, sequence-based scores derived from evolutionary history, and

SUBMITTER: Ngu L 

PROVIDER: S-EPMC7004355 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature