Human O‐phosphoethanolamine phospho‐lyase (hEtnppl; EC 4.2.3.2) is a pyridoxal 5′‐phosphate‐dependent enzyme that catalyzes the degradation of O‐phosphoethanolamine (PEA) into acetaldehyde, phosphate and ammonia. Physiologically, the enzyme is involved in phospholipid metabolism, as PEA is the precursor of phosphatidylethanolamine in the CDP‐ethanolamine (Kennedy) pathway. Here, the crystal structure of hEtnppl in complex with pyridoxamine 5′‐phosphate was determined at 2.05 Å resolution by molecular replacement using the structure of A1RDF1 from Arthrobacter aurescens TC1 (PDB entry 5g4i) as the search model. Structural analysis reveals that the two proteins share the same general fold and a similar arrangement of active‐site residues. These results provide novel and useful information for the complete characterization of the human enzyme.

中文翻译：

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人 O-磷酸乙醇胺磷酸裂合酶的结构表征。

人O -磷酸乙醇胺磷酸裂解酶 (hEtnppl; EC 4.2.3.2) 是一种吡哆醛 5'-磷酸依赖性酶，可催化O -磷酸乙醇胺 (PEA) 降解为乙醛、磷酸盐和氨。从生理学角度来说，该酶参与磷脂代谢，因为 PEA 是 CDP-乙醇胺 (Kennedy) 途径中磷脂酰乙醇胺的前体。在此，使用金节杆菌TC1（PDB 条目 5g4i）的 A1RDF1 结构作为搜索模型，通过分子替换以 2.05 Å 分辨率确定了 hEtnppl 与吡哆胺 5'-磷酸复合物的晶体结构。结构分析表明，这两种蛋白质具有相同的一般折叠和相似的活性位点残基排列。这些结果为人类酶的完整表征提供了新颖且有用的信息。