Flavin transferase: the maturation factor of flavin-containing oxidoreductases

Biochemical Society Transactions
Alexander V BogachevYulia V Bertsova

Abstract

Flavins, cofactors of many enzymes, are often covalently linked to these enzymes; for instance, flavin adenine mononucleotide (FMN) can form a covalent bond through either its phosphate or isoalloxazine group. The prevailing view had long been that all types of covalent attachment of flavins occur as autocatalytic reactions; however, in 2013, the first flavin transferase was identified, which catalyzes phosphoester bond formation between FMN and Na+-translocating NADH:quinone oxidoreductase in certain bacteria. Later studies have indicated that this post-translational modification is widespread in prokaryotes and is even found in some eukaryotes. Flavin transferase can occur as a separate ∼40 kDa protein or as a domain within the target protein and recognizes a degenerate DgxtsAT/S motif in various target proteins. The purpose of this review was to summarize the progress already achieved by studies of the structure, mechanism, and specificity of flavin transferase and to encourage future research on this topic. Interestingly, the flavin transferase gene (apbE) is found in many bacteria that have no known target protein, suggesting the presence of yet unknown flavinylation targets.

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Citations

Jun 9, 2019·Applied and Environmental Microbiology·Eric D KeesJeffrey A Gralnick
Dec 14, 2019·FEMS Microbiology Letters·Yulia V BertsovaAlexander V Bogachev
Sep 27, 2019·Current Drug Targets·Yoshimi Okamoto-UchidaJun Hirayama
Dec 11, 2019·Proceedings of the National Academy of Sciences of the United States of America·Samuel H LightDaniel A Portnoy
Oct 28, 2020·FEMS Microbiology Letters·Yulia V BertsovaAlexander V Bogachev
Jul 27, 2021·Bioconjugate Chemistry·Yapei TongMarco W Fraaije
Apr 28, 2020·The Journal of Physical Chemistry. a·Brian D EtzShubham Vyas
Nov 20, 2021·Protein Science : a Publication of the Protein Society·Ranjit K DekaChad A Brautigam

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