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Protein Dynamics in Living Cells

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

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Updated: Jun 12, 2025

Click-Chemistry Based Fluorometric Assay for Apolipoprotein N-acyltransferase from Enzyme Characterization to High-Throughput Screening

Click-Chemistry Based Fluorometric Assay for Apolipoprotein N-acyltransferase from Enzyme Characterization to High-Throughput Screening

Published on: May 13, 2020

Flavin transferase ApbE: From discovery to applications.

Xiaoman Fan¹, Marco W Fraaije¹

¹Molecular Enzymology, University of Groningen, Groningen, The Netherlands.

The Journal of Biological Chemistry

|March 28, 2025

Summary

ApbE is a unique enzyme that covalently attaches flavin cofactors to proteins, essential for bacterial function. This review explores ApbE

Area of Science:

Biochemistry
Molecular Biology
Enzymology

Background:

ApbE is a membrane-bound enzyme catalyzing covalent flavinylation, a vital posttranslational modification for bacterial protein function.
This modification is conserved across bacteria, archaea, and eukaryotes, highlighting its fundamental biological importance.
ApbE functions as a flavin transferase, attaching flavin mononucleotide to specific serine or threonine residues on target proteins.

Purpose of the Study:

To review the structural and mechanistic properties of ApbE.
To summarize recent applications of ApbE in protein modification.
To highlight the significance of ApbE-mediated flavinylation in bacterial metabolism and respiration.

Main Methods:

Structural analysis of ApbE domains (flavin-binding and catalytic).

Keywords:

FMN covalent flavinylation flavin transferase posttranslational modification

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Mechanistic studies on flavinylation process, including cofactor utilization and substrate recognition.

Review of experimental evidence for ApbE applications in protein engineering and flavoprotein modification.

Main Results:

ApbE recognizes specific protein motifs, mediating flavinylation dependent on magnesium and flavin adenine dinucleotide.
ApbE-catalyzed flavinylation is essential for key bacterial respiratory and metabolic pathways.
ApbE serves as a versatile tool for creating covalent flavoproteins and engineering protein modifications.

Conclusions:

ApbE is crucial for flavoprotein maturation through covalent flavinylation.
Further research is needed to elucidate the roles of uncharacterized ApbE targets and expand its applications.
ApbE holds significant potential as a biotechnological tool for protein engineering.