ArticlePloS one2017
Kinetic characterization of Vibrio cholerae ApbE: Substrate specificity and regulatory mechanisms.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- One-Pot Enzymatic ADDing of Click Chemistry Handles for Protein Immobilization and Bioconjugation of Small and Biomolecules.Bioconjugate chemistry · 2026Article
- Flavin transferase ApbE: From discovery to applications.The Journal of biological chemistry · 2025Review
- Structural insights into the catalytic and inhibitory mechanisms of the flavin transferase FmnB inMedComm · 2022Article
- Article
- Role of Subunit D in Ubiquinone-Binding Site ofACS omega · 2019Article
- Conserved residue His-257 ofThe Journal of biological chemistry · 2019Article
- Is there a Function for a Sex Pheromone Precursor?Journal of integrative bioinformatics · 2019Article
- Transcriptomic Identification and Biochemical Characterization of HmpA, a Nitric Oxide Dioxygenase, Essential for Pathogenesis ofFrontiers in microbiology · 2019Article
- Characterization of theThe Journal of biological chemistry · 2018Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
ApbE is a member of a novel family of flavin transferases that incorporates flavin mononucleotide (FMN) to subunits of diverse respiratory complexes, which fulfill important homeostatic functions. In this work a detailed characterization of Vibrio cholerae ApbE physiologic activity, substrate specificity and pH dependency was carried out. The data obtained show novel characteristics of the regulation and function of this family. For instance, our experiments indicate that divalent cations are essential for ApbE function, and that the selectivity depends largely on size and the coordination sphere of the cation. Our data also show that ApbE regulation by pH, ADP and potassium is an important mechanism that enhances the adaptation, survival and colonization of V. cholerae in the small intestine. Moreover, studies of the pH-dependency of the activity show that the reaction is favored under alkaline conditions, with a pKa of 8.4. These studies, together with sequence and structure analysis allowed us to identify His257, which is absolutely conserved in the family, as a candidate for the residue whose deprotonation controls the activity. Remarkably, the mutant H257G abolished the flavin transfer activity, strongly indicating that this residue plays an important role in the catalytic mechanism of ApbE.
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