Arginine kinase
| arginine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.3.3 | ||||||||
| CAS no. | 9026-70-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, arginine kinase (EC 2.7.3.3) is an enzyme that catalyzes the chemical reaction
- 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
[edit]The systematic name of this enzyme class is
- ATP:L-arginine Nω-phosphotransferase
Other names in common use include
- arginine phosphokinase,
- adenosine 5'-triphosphate: L-arginine phosphotransferase,
- adenosine 5'-triphosphate-arginine phosphotransferase,
- ATP:L-arginine N-phosphotransferasel ATP:L-arginine, and
- ω-N-phosphotransferase.
Function
[edit]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.
Structural studies
[edit]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
[edit]- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
Further reading
[edit]- Elodi P, Szorenyi E (1956). "Properties of crystalline arginine-phosphoferase isolated from Crustacean muscle". Acta Physiologica Academiae Scientiarum Hungaricae. 9 (4): 367–379. PMID 13339436.
- Morrison JF, Griffiths DE, Ennor AH (January 1957). "The purification and properties of arginine phosphokinase". The Biochemical Journal. 65 (1): 143–153. doi:10.1042/bj0650143. PMC 1199841. PMID 13403885.
- Urbancsek J, Fancsovits P, Akos M, Tóthné Gilán Z, Hauzman E, Papp Z (January 2006). "[In vitro fertilization at our department. A decade's work in figures and facts (1994-2003)]". Orvosi Hetilap. 147 (1): 7–14. PMID 16519065.
- Virden R, Watts DC, Baldwin E (March 1965). "Adenosine 5′-Triphosphate-Arginine Phosphotransferase from Lobster Muscle: Purification and Properties". The Biochemical Journal. 94 (3): 536–544. doi:10.1042/bj0940536. PMC 1206586. PMID 14340045.
