Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/59028
Type: Artigo de Periódico
Title: The role of remote flavin adenine dinucleotide pieces in the oxidative decarboxylation catalyzed by salicylate hydroxylase
Authors: Mozart Silvio Pereira
Simara Semíramis de Araújo
Ronaldo Alves Pinto Nagem
John P. Richard
Tiago Antônio da Silva Brandão
Abstract: 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.
Subject: Análise enzimática
Enzimas - Regulação
Cinética de enzimas
Mecanismos de reações orgânicas
Reações químicas
Bioquímica
language: eng
metadata.dc.publisher.country: Brasil
Publisher: Universidade Federal de Minas Gerais
Publisher Initials: UFMG
metadata.dc.publisher.department: ICB - DEPARTAMENTO DE BIOQUÍMICA E IMUNOLOGIA
ICX - DEPARTAMENTO DE QUÍMICA
Rights: Acesso Restrito
metadata.dc.identifier.doi: https://doi.org/10.1016/j.bioorg.2021.105561
URI: http://hdl.handle.net/1843/59028
Issue Date: 2022
metadata.dc.url.externa: https://www.sciencedirect.com/science/article/pii/S0045206821009391
metadata.dc.relation.ispartof: Bioorganic Chemistry
Appears in Collections:Artigo de Periódico

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