6TOR

human O-phosphoethanolamine phospho-lyase

6TOR の概要

• エントリーDOI: 10.2210/pdb6tor/pdb
• 分子名称: Ethanolamine-phosphate phospho-lyase, GLYCEROL, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• 機能のキーワード: o-phosphoethanolamine phospho-lyase, pyridoxal 5'-phosphate-dependent enzyme, phospholipid metabolism., lyase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 112564.41

構造登録者

Vettraino, C.,Donini, S.,Parisini, E. (登録日: 2019-12-11, 公開日: 2020-04-15, 最終更新日: 2024-01-24)

主引用文献

Vettraino, C.,Peracchi, A.,Donini, S.,Parisini, E.
Structural characterization of human O-phosphoethanolamine phospho-lyase.
Acta Crystallogr.,Sect.F, 76:160-167, 2020

PubMed Abstract: 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.

PubMed: 32254049
DOI: 10.1107/S2053230X20002988

実験手法

X-RAY DIFFRACTION (2.05 Å)