Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 552, Issue -, Pages 114-119Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2021.03.046
Keywords
AEP degradation pathway; PaAEPT; Pseudomonas aeruginosa; Crystal structure
Categories
Funding
- National Natural Science Foundation of China [31800627, 31870053]
- National Key Research and Development Program of China [2020YFC1807003]
Ask authors/readers for more resources
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.
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available