Structural characterization of human O-phosphoethanolamine phospho-lyase.
Acta Crystallogr F Struct Biol Commun
; 76(Pt 4): 160-167, 2020 Apr 01.
Article
em En
| MEDLINE
| ID: mdl-32254049
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 2.05â
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.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Carbono-Oxigênio Liases
Limite:
Humans
Idioma:
En
Revista:
Acta Crystallogr F Struct Biol Commun
Ano de publicação:
2020
Tipo de documento:
Article
País de afiliação:
Itália