Structural characterization of human O‐phosphoethanolamine phospho‐lyase. Issue 4 (7th April 2020)

• Record Type: Journal Article
• Authors: Vettraino, Chiara; Peracchi, Alessio; Donini, Stefano; Parisini, Emilio
• Is Part Of: Acta crystallographica. Volume 76:Issue 4(2020:Apr.)
• Page Start: 160
• Page End: 167
• Publication Date: 2020-04-07
• Subjects: O‐phosphoethanolamine phospho‐lyase -- lyases -- PMP -- crystal structure; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X20002988
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The crystal structure of human O ‐phosphoethanolamine phospho‐lyase, a pyridoxal 5′‐phosphate‐dependent enzyme that catalyzes the degradation of O ‐phosphoethanolamine (PEA) into acetaldehyde, phosphate and ammonia, is reported at 2.05 Å resolution. As PEA is the precursor of phosphatidylethanolamine in the CDP‐ethanolamine (Kennedy) pathway, the enzyme is physiologically involved in phospholipid metabolism. 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.