Structural characterization of a 2-aminoethylphosphonate:pyruvate aminotransferase from Pseudomonas aeruginosa PAO1

2-aminoethylphosphonate:pyruvate aminotransferase (AEPT) is a pyridoxal 5 '-phosphate (PLP)-dependent enzyme that mediates the first step in the AEP degradation pathway. It catalyzes the transamination of 2-aminoethylphosphonate (AEP) with pyruvate to phosphonoacetaldehyde and L-alanine respectively. Although the enzyme is widely present in microorganisms, there are few reports on the structure and function of AEPT to date. Here we report the crystal structure of AEPT from Pseudomonas aeruginosa PAO1 (PaAEPT) to 2.35 angstrom resolution in the absence of the PLP cofactor. PaAEPT crystallizes in space group P2(1)2(1)2 with one monomer per asymmetric unit. Analytical ultracentrifugation analysis shows that PaAEPT forms a stable dimer in solution. Our work provides a valuable starting point for further functional and mechanistic studies of the AEP degradation pathway. (C) 2021 Elsevier Inc. All rights reserved.

Automated summary

This study presents the crystal structure analysis of AEPT from Pseudomonas aeruginosa, revealing its catalytic mechanism in transamination as the first step in the AEP degradation pathway. The findings provide valuable insights for further functional and mechanistic studies of AEPT.