Carbohydrate deacetylase, a key enzyme in oxidative chitin degradation, is evolutionarily linked to amino acid deacetylase.

ABSTRACT: The microbial oxidative cleavage of chitin, the second most abundant biopolymer in nature, generates a substantial amount of oxidized amino sugar, 2-(acetylamino)-2-deoxy-D-gluconic acid (GlcNAc1A). The catabolism of GlcNAc1A is key to the oxidative chitin degradation pathway. However, the molecular mechanism and evolution underlying this pathway remain elusive. Here, we target OngB, which initiates the GlcNAc1A catabolism, to explore the molecular mechanism driving the evolution of this process. We characterized PpOngB (the OngB from Pseudoalteromonas prydzensis ACAM 620) and its homologs as specific deacetylases for GlcNAc1A and solved the structures of WT PpOngB and its inactive mutant in complex with GlcNAc1A. Structural, mutational, and biochemical analyses revealed that PpOngB utiliz

SUBMITTER: Wang JP 

PROVIDER: S-EPMC12017989 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature