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Strict reaction and substrate specificity of AGXT2L1, the human O ‐phosphoethanolamine phospho‐lyase
Author(s) -
Schiroli Davide,
Cirrincione Simona,
Donini Stefano,
Peracchi Alessio
Publication year - 2013
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.1178
Subject(s) - lyase , enzyme , substrate (aquarium) , gene , biochemistry , transaminase , chemistry , biology , ecology
Dysregulated expression of the AGXT2L1 gene has been associated to neuropsychiatric disorders. Recently the gene product was shown to possess O ‐phosphoethanolamine phospho‐lyase activity. We here analyze the specificity of AGXT2L1 in terms of both reaction and substrate. We show that the enzyme, despite having evolved from a transaminase ancestor, is at least 500‐fold more active as a lyase than as an aminotransferase. Furthermore, the lyase reaction is very selective for O ‐phosphoethanolamine, strongly discriminating against closely related compounds, and we dissect the factors that contribute to such narrow substrate specificity. Overall, AGXT2L1 function appears to be rigidly confined to phospholipid metabolism, which is altered in neuropsychiatric disturbances. © 2013 IUBMB Life, 65(7):645–650, 2013.