Catalytically important flavin linked through a phosphoester bond in a eukaryotic fumarate reductase

One of the three domains of kinetoplastid NADH:fumarate oxidoreductase (FRD) is homologous to bacterial flavin transferase that catalyzes transfer of FMN residue from FAD to threonine in flavoproteins. Leptomonas pyrrhocoris FRD produced in yeast cells, which lack flavin transferase gene in their pr...

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Bibliographic Details
Published in:Biochimie 2018-06, Vol.149, p.34-40
Main Authors: Serebryakova, Marina V., Bertsova, Yulia V., Sokolov, Svyatoslav S., Kolesnikov, Alexander A., Baykov, Alexander A., Bogachev, Alexander V.
Format: Article
Language:English
Subjects:
Amino Acid Sequence - genetics
ApbE
Catalysis
Escherichia coli - genetics
Eukaryota - enzymology
Flavin mononucleotide
Flavins - chemistry
Flavoproteins - chemistry
Flavoproteins - genetics
Kinetoplastida
NADH:Fumarate oxidoreductase
Oxidation-Reduction
Post-translational modification
Protein Binding - genetics
Protein Domains
Succinate Dehydrogenase - chemistry
Succinate Dehydrogenase - genetics
Trypanosomatina - enzymology
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Summary:One of the three domains of kinetoplastid NADH:fumarate oxidoreductase (FRD) is homologous to bacterial flavin transferase that catalyzes transfer of FMN residue from FAD to threonine in flavoproteins. Leptomonas pyrrhocoris FRD produced in yeast cells, which lack flavin transferase gene in their proteome, reduces fumarate in the presence of NADH and contains an FMN residue covalently linked to a Ser9 residue. The conserved flavinylation motif of FRD, D3(g/s)x(s/t)(s/g)AS9, is similar to the Dxx(s/t)gAT motif recognized by flavin transferase in prokaryotic proteins. Ser9 replacement abolished the flavinylation and fumarate reductase activity of FRD. These findings suggest that the flavinylation is important for the activity of FRD and that this post-translational modification is carried out by the own flavin transferase domain. •Kinetoplastid NADH:fumarate oxidoreductase contains a covalently bound FMN residue.•The FMN residue forms a phosphoester with Ser9 and is essential for enzyme activity.•One of the three domains of the enzyme is homologous to bacterial flavin transferase.•This domain supposedly forms the flavin-binding site and catalyzes Ser9 flavinylation.
ISSN:0300-9084
1638-6183
DOI:10.1016/j.biochi.2018.03.013