7E7G

2-aminoethylphosphonate:pyruvate aminotransferase (AEPT) native

7E7G の概要

• エントリーDOI: 10.2210/pdb7e7g/pdb
• 分子名称: 2-aminoethylphosphonate--pyruvate transaminase (2 entities in total)
• 機能のキーワード: aep degradation pathway, paaept, pseudomonas aeruginosa, crystal structure., transferase
• 由来する生物種: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40466.45

構造登録者

Jia, H.,Zhang, Q.,Bartlam, M. (登録日: 2021-02-26, 公開日: 2021-03-31, 最終更新日: 2023-11-29)

主引用文献

Jia, H.,Chen, Y.,Chen, Y.,Liu, R.,Zhang, Q.,Bartlam, M.
Structural characterization of a 2-aminoethylphosphonate:pyruvate aminotransferase from Pseudomonas aeruginosa PAO1.
Biochem.Biophys.Res.Commun., 552:114-119, 2021

PubMed Abstract: 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 Å resolution in the absence of the PLP cofactor. PaAEPT crystallizes in space group P222 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.

PubMed: 33743347
DOI: 10.1016/j.bbrc.2021.03.046

実験手法

X-RAY DIFFRACTION (2.35 Å)