Lysine malonylation is a type of protein acylation modification that has been founded in eukaryotes and bacteria.
Protein malonylation is the reversible addition of a malonyl group into a lysine residue, regulating protein
stability, protein localization, enzyme activity, and so on. The regulatory role of lysine malonylation in many
biological processes has been established in a variety of organisms such as affecting mitochondrial function, fatty
acid synthesis, and energy metabolism. Given the potential importance of lysine malonylation, the identification and
investigation of lysine malonylation sites are extremely urgent and may provide useful information for biomedical
research. Creative Proteomics offers the lysine malonylation analysis service to identify
malonylated proteins and lysine malonylation sites in proteins. We specialize in the analysis and identification of
protein post-translational modifications (PTMs) based on high-resolution mass spectrometry (MS), aiming to provide
quality and efficient solutions for our customers' research projects.
Protein malonylation
Lysine malonylation was first discovered in 2011 in mammals and Escherichia coli. This type of acylation
modification requires malonyl-coenzyme A (CoA) as a substrate to be added to lysine residues, modulating protein
structure and function by interfering with electrostatic interactions. As an evolutionarily conserved acyl
modification, Lysine malonylation has been found to take part in modulating various cellular processes. Lysine
malonylation is abundant in mitochondrial proteins that regulate metabolic pathways (e.g. glycolysis, fatty acid
oxidation, and inflammation) in animal cells (e.g. endothelial cells and macrophages). Lysine malonylation has been
reported to play an important role in metabolic processes and stress responses, and is closely associated with
angiogenesis-related diseases, fatty acid oxidation, the associated genetic disease, and metabolic diseases (such as
diabetes and inflammation).
Fig. 1 Production of
malonyl-CoA and its regulation in malonylation. (Lu Zou, et al., 2022)
Malonylation proteomics analysis
Due to the limitations of experimental techniques, it is a great challenge to fast and accurately identify
malonylation sites. Creative Proteomics combines affinity enrichment and liquid
chromatography-tandem mass spectrometry (LC-MS/MS) analysis to provide comprehensive and accurate identification of
lysine malonylated proteins and lysine malonylation sites in mammalian and plant cells. With our well-established
platform, we can help our customers achieve the following lists:
- Identification of lysine malonylated proteins.
- Functional annotation of malonylated proteins.
- Identification and analysis of lysine malonylated sites.
- Prediction of species-specific malonylation sites.
Workflow of protein malonylation analysis
- Protein extraction and digestion.
- HPLC fractionation.
- Affinity enrichment.
- LC-MS/MS analysis.
- Data research and analysis.
- Bioinformatics analysis.
Sample requirements
- Acceptable samples: Protein extracts, cell samples, tissue samples, and microorganism samples.
- Sample shipping: Sufficient amount of dry ice for shipping, or consult our technical staff before sending
samples.
- Before the formal experiment, we will always test the samples you provide.
Protein malonylation is an important member of the large family of acyl modifications. With continuous research,
malonylation modifications have been found to be widely involved in important life activities of the organism, and
gradually become a hot research topic in the life science field. You only need to place an order and send samples,
we provide a one-stop protein malonylation analysis service. Please contact us
if you are interested. We are looking forward to cooperating with you.
References
- Colak, Gozde, et al. "Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic
Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation [S]." Molecular
& Cellular Proteomics 14.11 (2015): 3056-3071.
- Lu Zou, et al. "Lysine Malonylation and Its Links to Metabolism and Diseases." Aging and
disease. 2022.
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