Mining the Flavoproteome of Brucella ovis, the Brucellosis Causing Agent in Ovis aries

Minjárez-Sáenz, Martha; Martínez‐Júlvez, Marta; Yruela, Inmaculada; Medina, Milagros

doi:10.1128/spectrum.02294-21

Cited by 3 publications

(1 citation statement)

References 132 publications

(141 reference statements)

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“…Flavoproteins are a diverse class of proteins, mostly enzymes, that contain flavin mononucleotide (FMN) or flavin adenine dinucleotide (FAD) as cofactors, which enable them to participate in a wide range of relevant processes for the homeostasis of living beings. While some organisms rely heavily on flavin-dependent activities, others maintain them to a minimum ( Macheroux et al, 2011 ; Lienhart et al, 2013 ; Gudipati et al, 2014 ; Schall et al, 2020 ; Eggers et al, 2021 ; Minjárez-Sáenz et al, 2022 ). Nonetheless, flavoproteins account for ∼2.5–5% of the proteome of each species, with a clear bypass for the use of FAD over FMN.…”

Section: Introductionmentioning

confidence: 99%

Riboflavin kinase and pyridoxine 5′-phosphate oxidase complex formation envisages transient interactions for FMN cofactor delivery

Rivero

Boneta²,

Novo³

et al. 2023

Front. Mol. Biosci.

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Enzymes catalysing sequential reactions have developed different mechanisms to control the transport and flux of reactants and intermediates along metabolic pathways, which usually involve direct transfer of metabolites from an enzyme to the next one in a cascade reaction. Despite the fact that metabolite or substrate channelling has been widely studied for reactant molecules, such information is seldom available for cofactors in general, and for flavins in particular. Flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) act as cofactors in flavoproteins and flavoenzymes involved in a wide range of physiologically relevant processes in all type of organisms. Homo sapiens riboflavin kinase (RFK) catalyses the biosynthesis of the flavin mononucleotide cofactor, and might directly interplay with its flavin client apo-proteins prior to the cofactor transfer. Non-etheless, none of such complexes has been characterized at molecular or atomic level so far. Here, we particularly evaluate the interaction of riboflavin kinase with one of its potential FMN clients, pyridoxine-5′-phosphate oxidase (PNPOx). The interaction capacity of both proteins is assessed by using isothermal titration calorimetry, a methodology that allows to determine dissociation constants for interaction in the micromolar range (in agreement with the expected transient nature of the interaction). Moreover, we show that; i) both proteins become thermally stabilized upon mutual interaction, ii) the tightly bound FMN product can be transferred from RFK to the apo-form of PNPOx producing an efficient enzyme, and iii) the presence of the apo-form of PNPOx slightly enhances RFK catalytic efficiency. Finally, we also show a computational study to predict likely RFK-PNPOx binding modes that can envisage coupling between the FMN binding cavities of both proteins for the potential transfer of FMN.

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Section: Introductionmentioning

confidence: 99%

Riboflavin kinase and pyridoxine 5′-phosphate oxidase complex formation envisages transient interactions for FMN cofactor delivery

Rivero

Boneta²,

Novo³

et al. 2023

Front. Mol. Biosci.

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New insights into the function and molecular mechanisms of Ferredoxin-NADP+ reductase from Brucella ovis

Moreno,

Quereda-Moraleda,

Lozano-Vallhonrat

et al. 2024

Archives of Biochemistry and Biophysics

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Mechanistic and structural insights into vitamin B2 metabolizing enzyme riboflavin kinase from Leishmania donovani

Roy,

Paul,

Khandibharad

et al. 2024

International Journal of Biological Macromolecules

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Mining the Flavoproteome of Brucella ovis, the Brucellosis Causing Agent in Ovis aries

Abstract: Some microorganisms depend heavily on flavin-dependent activities, but others maintain them at a minimum. Knowledge about flavoprotein content and functions in different microorganisms will help to identify their metabolic requirements, as well as to benefit either industry or health.

Cited by 3 publications

References 132 publications

Riboflavin kinase and pyridoxine 5′-phosphate oxidase complex formation envisages transient interactions for FMN cofactor delivery

Riboflavin kinase and pyridoxine 5′-phosphate oxidase complex formation envisages transient interactions for FMN cofactor delivery

New insights into the function and molecular mechanisms of Ferredoxin-NADP+ reductase from Brucella ovis

Mechanistic and structural insights into vitamin B2 metabolizing enzyme riboflavin kinase from Leishmania donovani

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