Revisiting the Roles of Catalytic Residues in Human Ornithine Transcarbamylase.

ABSTRACT: Human ornithine transcarbamylase (hOTC) is a mitochondrial transferase protein involved in the urea cycle and is crucial for the conversion of toxic ammonia to urea. Structural analysis coupled with kinetic studies of Escherichia coli, rat, bovine, and other transferase proteins has identified residues that play key roles in substrate recognition and conformational changes but has not provided direct evidence for all of the active residues involved in OTC function. Here, computational methods were used to predict the likely active residues of hOTC; the function of these residues was then probed with site-directed mutagenesis and biochemical characterization. This process identified previously reported active residues, as well as distal residues that contribute to activity. Mutation

SUBMITTER: Watson SS 

PROVIDER: S-EPMC11256359 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature