State Key Laboratory of Medicinal Chemical Biology, Tianjin Key Laboratory of Protein Science and College of Life Sciences, Nankai University, Tianjin, 300071, China.
State Key Laboratory of Medicinal Chemical Biology, Tianjin Key Laboratory of Protein Science and College of Life Sciences, Nankai University, Tianjin, 300071, China.
Biochem Biophys Res Commun. 2021 May 7;552:114-119. doi: 10.1016/j.bbrc.2021.03.046. Epub 2021 Mar 18.
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.
2-氨基乙基膦酸盐：丙酮酸氨基转移酶（AEPT）是一种依赖于吡哆醛 5'-磷酸（PLP）的酶，介导 AEP 降解途径的第一步。它催化 2-氨基乙基膦酸盐（AEP）与丙酮酸分别转氨生成膦羟乙醛和 l-丙氨酸。尽管该酶广泛存在于微生物中，但迄今为止，关于 AEPT 的结构和功能的报道很少。在这里，我们报道了铜绿假单胞菌 PAO1（PaAEPT）中 AEPT 的晶体结构，分辨率为 2.35Å，没有 PLP 辅因子。PaAEPT 以 P222 空间群结晶，每个不对称单元中有一个单体。分析超速离心分析表明，PaAEPT 在溶液中形成稳定的二聚体。我们的工作为进一步研究 AEP 降解途径的功能和机制提供了有价值的起点。
