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B6db references: 23761375

type Journal Article
authors Schiroli, D.; Cirrincione, S.; Donini, S.; Peracchi, A.
title Strict reaction and substrate specificity of AGXT2L1, the human O-phosphoethanolamine phospho-lyase
journal IUBMB Life
sel selected
ui 23761375
year (2013)
volume 65
number 7
pages 645-50
keywords doi: 10.1002/iub.1178
abstract 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.
last changed 2016/10/03 12:40

B6db references