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| Description: Tyrosine is hydroxylated to p-hydroxyphenylpyruvate catalyzed by p-hydroxyphenylpyruvate dioxygenase, an unusual iron-containing enzyme, which catalyzes a ring hydroxylation, decarboxylation, and side chain migration, using ascorbate as a cofactor. Procollagen prolyl hydroxylase catalyzes the same chemistry. This reaction involves a mechanism called the NIH shift, after scientists at the NIH, who described a ring hydroxylation that proceeds via formation of an epoxide intermediate and migration of the alkyl side chain. Picture Stats: Views: 105 Filesize: 54.74kB Height: 216 Width: 1033 Source: https://biology-forums.com/index.php?action=gallery;sa=view;id=34776 |