Flavogenomics – a genomic and structural view of flavin‐dependent proteins

@article{Macheroux2011FlavogenomicsA,
  title={Flavogenomics – a genomic and structural view of flavin‐dependent proteins},
  author={Peter Macheroux and Barbara Kappes and Steven E. Ealick},
  journal={The FEBS Journal},
  year={2011},
  volume={278}
}
Riboflavin (vitamin B2) serves as the precursor for FMN and FAD in almost all organisms that utilize the redox‐active isoalloxazine ring system as a coenzyme in enzymatic reactions. The role of flavin, however, is not limited to redox processes, as ∼ 10% of flavin‐dependent enzymes catalyze nonredox reactions. Moreover, the flavin cofactor is also widely used as a signaling and sensing molecule in biological processes such as phototropism and nitrogen fixation. Here, we present a study of 374… 
Flavin transferase: the maturation factor of flavin-containing oxidoreductases.
TLDR
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.
The Flavoproteome of the Model Plant Arabidopsis thaliana
TLDR
This paper intends to compile all potential FAD/FMN-binding proteins encoded by the genome of Arabidopsis thaliana to reflect presumably their need for differential transcriptional control or the expression of similar proteins with modified flavin-binding properties or catalytic activities.
Mechanistic and biocatalytic enzymology of flavoprotein oxidases
TLDR
The role of two tyrosine residues play a crucial role in enabling substrate activation by VAO, both by stimulating preferential binding of the phenolate form of the substrate and by deprotonating the substrate when it is bound in its protonated form.
Structural and Functional Characterization of a Short-Chain Flavodoxin Associated with a Noncanonical 1,2-Propanediol Utilization Bacterial Microcompartment.
TLDR
Structural and functional results suggest that PDU1C BMCs encapsulate Fld1C to store and transfer electrons for the reactivation and/or recycling of the B12 cofactor utilized by the signature enzyme.
Efficient flavinylation of glycosomal fumarate reductase by its own ApbE domain in Trypanosoma brucei
TLDR
How the higher efficiency due to unusual fusion of the ApbE domain to its substrate protein FRD may provide a selective advantage by faster FRD biogenesis during rapid metabolic adaptation of trypanosomes is discussed.
From cholesterogenesis to steroidogenesis: role of riboflavin and flavoenzymes in the biosynthesis of vitamin D.
TLDR
Overall, a deeper understanding of the role of riboflavin in these pathways may prove essential to targeted therapeutic designs aimed at cholesterol and vitamin D metabolism.
Riboflavin transport and metabolism in humans
TLDR
The molecular and functional studies of transporters and enzymes herereported, provide guidelines for improving therapies which may have beneficial effects on the altered metabolism and improve the molecular description of human pathologies.
Kinetic and Structural Studies on Flavin-dependent Enzymes involved in Glycine Betaine Biosynthesis and Propionate 3-nitronate Detoxification
TLDR
The crystal structure of choline oxidase in complex with glycine betaine was solved and the roles of the residue F357 in the oxidative half reaction investigated by combination of steady state kinetics, rapid kinetic, pH, mutagenesis, substrate deuterium and solvent isotope effects, viscosity effects and molecular dynamics simulations.
Overview of flavin-dependent enzymes.
...
...

References

SHOWING 1-10 OF 80 REFERENCES
A genomic overview of pyridoxal‐phosphate‐dependent enzymes
TLDR
In many free‐living prokaryotes, almost 1.5% of all genes code for PLP‐dependent enzymes, but in higher eukaryotes the percentage is substantially lower, consistent with these catalysts being involved mainly in basic metabolism.
Dodecin Is the Key Player in Flavin Homeostasis of Archaea
TLDR
In vitro and in vivo data are presented showing that the recently discovered archaeal dodecin is an RfBP, and it is revealed that riboflavin storage is not restricted to eukaryotes, and the different structural and functional properties of a homologous bacterial dodECin suggest that dodec in has different roles in different kingdoms of life.
The diverse roles of flavin coenzymes--nature's most versatile thespians.
TLDR
This Perspective highlights the chemical versatility of flavins by reviewing research on five flavoenzymes that have been studied in the laboratory and finding that two catalytic mechanisms of two of these enzymes may involve novel flavin chemistry.
Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology.
TLDR
Current knowledge on the structure, enzymology, genetics, regulation and pathophysiology of mammalian molybdo-flavoenzymes is summarized.
Biochemical Evidence That Berberine Bridge Enzyme Belongs to a Novel Family of Flavoproteins Containing a Bi-covalently Attached FAD Cofactor*
TLDR
Overall, BBE is shown to exhibit typical flavoprotein oxidase properties as exemplified by the occurrence of an anionic flavin semiquinone species and formation of a flavin N(5)-sulfite adduct.
Unifying concepts in flavin-dependent catalysis.
TLDR
The results of the present study demonstrate that increasing the reactivity of the substrate and/or cofactor may be another important mechanism to decrease the activation barrier of a chemical reaction.
A single flavoprotein, AppA, integrates both redox and light signals in Rhodobacter sphaeroides
TLDR
AppA is the first example of a protein with dual sensing capabilities that integrates both redox and light signals and is likely to act as the photoreceptor for blue light‐dependent repression during continuous illumination.
The growing VAO flavoprotein family.
...
...