Arginine kinase

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arginine kinase
Identifiers
EC no. 2.7.3.3
CAS no. 9026-70-4
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MetaCyc metabolic pathway
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In enzymology, arginine kinase (EC 2.7.3.3) is an enzyme that catalyzes the chemical reaction

Contents

ATP + L-arginine ADP + Nω-phospho-L-arginine

Thus, the two substrates of this enzyme are ATP and L-arginine, whereas its two products are ADP and Nω-phospho-L-arginine. Unlike the phosphoester bond, formed during the phosphorylation of serine, threonine or tyrosine residues, the phosphoramidate (P-N bond) in phospho-arginine is unstable at low pH (<8), making it difficult to detect with the traditional mass spectrometry protocols. [1]

Arginine kinase belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. This enzyme participates in arginine and proline metabolism.

Nomenclature

The systematic name of this enzyme class is

Other names in common use include

Function

In Gram-positive bacteria, such as Bacillus subtilis , the arginine kinase McsB phosphorylates the arginine residues on incorrectly folded or aggregated proteins to target them for degradation by the bacterial protease ClpC-ClpP (ClpCP).The phospho-arginine (pArg) modification is recognised by the N-terminal domain of ClpC, the protein-unfolding subunit of the ClpCP protease. Following recognition, the target protein is degraded by the ClpP subunit which has protease activity. Since phosphorylation reverses arginine's charge, the pArg modification has an unfolding effect on the target protein, easing its proteolytic degradation. Arginine phosphorylation is a dynamic post-translational modification, which can also be reversed by pArg-specific phosphatases, such as the bacterial YwlE. The pArg-ClpCP mechanism for protein degradation in bacteria is analogous to the eukaryotic ubiquitin-proteasome system. [2]

Several studies have reported the presence of arginine kinases in eukaryotes. [3] [4] A recent study identified arginine phosphorylation on 118 proteins in Jurkat cells, which were primarily proteins with DNA/RNA-binding activities. [5] The function of arginine phosphorylation in eukaryotes however is still unknown.

Arginine kinase as an allergen

Recent research has identified arginine kinase as a major panallergen in invertebrates, including edible insects such as the yellow mealworm (*Tenebrio molitor*). This enzyme can act as an IgE-binding allergen, and sensitization to arginine kinase may result in allergic reactions in individuals already sensitized to homologous proteins from other arthropods (e.g., crustaceans, mites). Cross-reactivity mediated by IgE antibodies has been observed between arginine kinase from edible insects and allergens in shrimp and house dust mites, which means clinical reactions may occur even upon first exposure. The emergence of edible insects in the human diet highlights the importance of arginine kinase in assessing the allergenic risks of novel food proteins. [6]

Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1BG0 , 1M15 , 1M80 , 1P50 , 1P52 , 1RL9 , 1SD0 , and 2J1Q .

References

  1. Elsholz AK, Turgay K, Michalik S, Hessling B, Gronau K, Oertel D, et al. (May 2012). "Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis". Proceedings of the National Academy of Sciences of the United States of America. 109 (19): 7451–7456. Bibcode:2012PNAS..109.7451E. doi: 10.1073/pnas.1117483109 . PMC   3358850 . PMID   22517742.
  2. Trentini DB, Suskiewicz MJ, Heuck A, Kurzbauer R, Deszcz L, Mechtler K, Clausen T (November 2016). "Arginine phosphorylation marks proteins for degradation by a Clp protease". Nature. 539 (7627): 48–53. Bibcode:2016Natur.539...48T. doi:10.1038/nature20122. PMC   6640040 . PMID   27749819.
  3. Levy-Favatier F, Delpech M, Kruh J (August 1987). "Characterization of an arginine-specific protein kinase tightly bound to rat liver DNA". European Journal of Biochemistry. 166 (3): 617–621. doi: 10.1111/j.1432-1033.1987.tb13558.x . PMID   3609029.
  4. Wakim BT, Aswad GD (January 1994). "Ca(2+)-calmodulin-dependent phosphorylation of arginine in histone 3 by a nuclear kinase from mouse leukemia cells". The Journal of Biological Chemistry. 269 (4): 2722–2727. doi: 10.1016/s0021-9258(17)42003-5 . PMID   8300603. S2CID   25969282.
  5. Fu S, Fu C, Zhou Q, Lin R, Ouyang H, Wang M, et al. (March 2020). "Widespread arginine phosphorylation in human cells - a novel protein PTM revealed by mass spectrometry" (PDF). Science China Chemistry. 63 (3): 341–346. doi:10.1007/s11426-019-9656-7. S2CID   211217421.
  6. Majsiak, Emilia; Choina, Magdalena; Gromek, Weronika; Wykrota, Julia; Kozłowska, Danuta; Swadźba, Jakub; Cukrowska, Bożena; Kowal, Krzysztof (2025). "IgE-based analysis of sensitization and cross-reactivity to yellow mealworm and edible insect allergens before their widespread dietary introduction". Scientific Reports. 15: 1466. doi:10.1038/s41598-024-83645-4.{{cite journal}}: CS1 maint: multiple names: authors list (link)

Further reading