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http://hdl.handle.net/1843/59028| Tipo: | Artigo de Periódico |
| Título: | The role of remote flavin adenine dinucleotide pieces in the oxidative decarboxylation catalyzed by salicylate hydroxylase |
| Autor(es): | Mozart Silvio Pereira Simara Semíramis de Araújo Ronaldo Alves Pinto Nagem John P. Richard Tiago Antônio da Silva Brandão |
| Resumen: | Salicylate hydroxylase (NahG) has a single redox site in which FAD is reduced by NADH, the O2 is activated by the reduced flavin, and salicylate undergoes an oxidative decarboxylation by a C(4a)-hydroperoxyflavin intermediate to give catechol. We report experimental results that show the contribution of individual pieces of the FAD cofactor to the observed enzymatic activity for turnover of the whole cofactor. A comparison of the kinetic parameters and products for the NahG-catalyzed reactions of FMN and riboflavin cofactor fragments reveal that the adenosine monophosphate (AMP) and ribitol phosphate pieces of FAD act to anchor the flavin to the enzyme and to direct the partitioning of the C(4a)-hydroperoxyflavin reaction intermediate towards hydroxylation of salicylate. The addition of AMP or ribitol phosphate pieces to solutions of the truncated flavins results in a partial restoration of the enzymatic activity lost upon truncation of FAD, and the pieces direct the reaction of the C(4a)-hydroperoxyflavin intermediate towards hydroxylation of salicylate. |
| Asunto: | Análise enzimática Enzimas - Regulação Cinética de enzimas Mecanismos de reações orgânicas Reações químicas Bioquímica |
| Idioma: | eng |
| País: | Brasil |
| Editor: | Universidade Federal de Minas Gerais |
| Sigla da Institución: | UFMG |
| Departamento: | ICB - DEPARTAMENTO DE BIOQUÍMICA E IMUNOLOGIA ICX - DEPARTAMENTO DE QUÍMICA |
| Tipo de acceso: | Acesso Restrito |
| Identificador DOI: | https://doi.org/10.1016/j.bioorg.2021.105561 |
| URI: | http://hdl.handle.net/1843/59028 |
| Fecha del documento: | 2022 |
| metadata.dc.url.externa: | https://www.sciencedirect.com/science/article/pii/S0045206821009391 |
| metadata.dc.relation.ispartof: | Bioorganic Chemistry |
| Aparece en las colecciones: | Artigo de Periódico |
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