2. Academic Validation
  3. Tyrosine nitration moderates the peptidase activity of human methionyl aminopeptidase 2

Tyrosine nitration moderates the peptidase activity of human methionyl aminopeptidase 2

  • Biochem Biophys Res Commun. 2013 Oct 11;440(1):37-42. doi: 10.1016/j.bbrc.2013.09.035.
John Y Ng 1,  Joyce Chiu,  Philip J Hogg,  Jason W H Wong
Affiliations

Affiliation

  • 1 Lowy Cancer Research Centre and the Prince of Wales Clinical School, University of New South Wales, Sydney, NSW 2052, Australia.
PMID: 24041691 DOI: 10.1016/j.bbrc.2013.09.035
Abstract

Methionyl Aminopeptidase 2 (MetAP2) plays an important role in the regulation of angiogenesis. This study examined whether nitration of MetAP2 alters its enzymatic activity in vitro. The activity of unmodified, nitrated and oxidised MetAP2 was assessed and it was found that nitration significantly reduced its ability to cleave a chromogenic substrate. Mass spectrometry analysis identified Tyr336 as a nitrated residue in MetAP2. Structural and evolutionary analysis indicate that this is an important residue for MetAP2 activity. Combined, the results show that the activity of MetAP2 is reduced by nitration and raise the possibility that nitration of MetAP2 is a mechanism contributing to endothelial dysfunction.

Keywords

Endothelial dysfunction; Methionyl aminopeptidase 2; Nitration; Nitrotyrosine.

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