Mutation of a conserved anthranilate phosphoribosyltransferase active site residue supports tryptophan biosynthesis in vivo

2025/11/03 by Stephen Klepin, Brooke Michalik, Lorraine Pillus +1
Biochemistry, Genetics and Molecular Biology · Materials Science · Medicine · #Biochemical and Molecular Research #Enzyme Structure and Function #Peptidase Inhibition and Analysis

paper · doi:10.17912/micropub.biology.001925

openalex publication_date 2025/11/03 · openalex created_date 2025/12/16 · openalex updated_date 2026/07/01

Abstract

functions. These findings add functional complexity to the Trp4 active site beyond crystallographic characterization.

Related

• Evolution of substrate specificity in a retained enzyme driven by gene loss
• Tryptophan metabolism in health and disease
• Protein phosphatase 4 – from obscurity to vital functions
• Delayed protein translocation protects mitochondria against toxic CAT-tailed proteins
• The crystal structures of apo and tryptophan-bound tryptophanyl-tRNA synthetase from Neisseria gonorrhoeae