Related Experiment Video
Updated: Feb 27, 2026

14:04
Viral Nanoparticles for In vivo Tumor Imaging
Published on: November 16, 2012
17.8K
The VAO/PCMH flavoprotein family
Tom A Ewing1, Marco W Fraaije2, Andrea Mattevi3
1Laboratory of Biochemistry, Wageningen University & Research, Stippeneng 4, 6708 WE Wageningen, The Netherlands.
Archives of Biochemistry and Biophysics
|July 4, 2017
Summary
The VAO/PCMH flavoprotein family, crucial for diverse reactions, has been phylogenetically divided into 11 subgroups. This research details their properties, new discoveries, and mechanistic insights, highlighting future research directions.
Area of Science:
- Biochemistry
- Enzymology
- Structural Biology
Background:
- The Vanillyl-alcohol oxidase/Primary-culture-medium-hydrolyzing enzyme (VAO/PCMH) flavoprotein family comprises structurally similar flavin-dependent enzymes.
- These enzymes share a conserved FAD-binding domain and a variable substrate-binding domain, allowing diverse substrate interactions while maintaining a common cofactor-binding fold.
Purpose of the Study:
- To provide a comprehensive overview of the VAO/PCMH flavoprotein family.
- To classify family members based on phylogenetic analysis and discuss their properties.
- To highlight recent discoveries and mechanistic advancements, identifying future research avenues.
Main Methods:
- Phylogenetic analysis of VAO/PCMH family members.
- Review of existing literature on enzyme properties, substrate specificities, and reaction mechanisms.
- Identification and characterization of newly discovered family members.
Main Results:
- The VAO/PCMH family was divided into 11 distinct subgroups based on phylogenetic analysis.
- Detailed discussion of the properties and known functions of each subgroup.
- Recent advances in understanding new members and enzymatic mechanisms were presented.
Conclusions:
- The phylogenetic classification provides a framework for understanding the diversity within the VAO/PCMH family.
- Ongoing research continues to expand the known members and mechanistic understanding of these flavoproteins.
- Significant open questions remain, offering opportunities for future biochemical and enzymological investigations.
More Related Videos
Related Concept Videos
COP Coated Vesicles
18.4K
Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of...
18.4K
Membrane Proteins
31.0K
Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
31.0K
Clathrin Coated Vesicles
9.8K
Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
9.8K
Phosphoinositides and PIPs
10.4K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
10.4K
Protein Families
4.6K
4.6K
Protein Families
17.3K
Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism. Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members. If these new proteins contain similar amino acids in key...
17.3K

