6TOR

human O-phosphoethanolamine phospho-lyase

Summary for 6TOR

• Entry DOI: 10.2210/pdb6tor/pdb
• Descriptor: Ethanolamine-phosphate phospho-lyase, GLYCEROL, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• Functional Keywords: o-phosphoethanolamine phospho-lyase, pyridoxal 5'-phosphate-dependent enzyme, phospholipid metabolism., lyase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 112564.41

Authors

Vettraino, C.,Donini, S.,Parisini, E. (deposition date: 2019-12-11, release date: 2020-04-15, Last modification date: 2024-01-24)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.05 Å)