Article
Peroxynitrite-induced nitration of tyrosine hydroxylase: identification of tyrosines 423, 428, and 432 as sites of modification by matrix-assisted laser desorption ionization time-of-flight mass spectrometry and tyrosine-scanning mutagenesis.
The Journal of biological chemistry - 19 Apr 2002
Kuhn Donald M, Sadidi Mahdieh, Liu Xiuli, Kreipke Christian, Geddes Timothy, Borges Chad, Watson J Throck
Abstract excerpt
Tyrosine hydroxylase (TH), the initial and rate-limiting enzyme in the biosynthesis of the neurotransmitter dopamine, is inactivated by peroxynitrite. The sites of peroxynitrite-induced tyrosine nitration in TH have been identified by matrix-assisted laser desorption time-of-flight mass spectrome...
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