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• W2086354788 startingPage "155" @default.
• W2086354788 abstract "There is increasing evidence that sequence-specific formation of 3-nitrotyrosine (3-NT) may cause functional changes in target proteins. Recently, the nitration of Tyr residues in glycogen phosphorylase b (Ph-b) was implicated in the age-associated decline of protein function [Sharov et al., Exp. Gerontol. 41 (2006) 407-416]; in another report, the nitration of one specific residue, Tyr613, located in the allosteric inhibition site was hypothesized as a rationale for peroxynitrite inactivation [Dairou et al., J. Mol. Biol. 372 (2007) 1009-1021]. In this study, we have optimized the analysis of in-gel Ph-b digests by high performance liquid chromatography-electro spray ionization-tandem mass spectrometry, in order to achieve a quantitative analysis of nitration of individual Tyr residues at a high coverage of Tyr-containing sequences (92%). Our data do not confirm the role of Tyr613 nitration in the control of enzymatic function. Furthermore, we show here that the enzymatic activity of Ph-b does not directly correlate with the protein nitration levels, and that the modification of Cys and, potentially, other amino acid residues can better rationalize Ph-b inactivation by peroxynitrite." @default.
• W2086354788 created "2016-06-24" @default.
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• W2086354788 date "2009-04-01" @default.
• W2086354788 modified "2023-10-03" @default.
• W2086354788 title "Inactivation of rabbit muscle glycogen phosphorylase b by peroxynitrite revisited: Does the nitration of Tyr613 in the allosteric inhibition site control enzymatic function?" @default.
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• W2086354788 doi "https://doi.org/10.1016/j.abb.2008.12.012" @default.
• W2086354788 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2774826" @default.
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• W2086354788 hasPublicationYear "2009" @default.
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