The Enzyme Database

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EC 3.9.1.2     
Accepted name: protein arginine phosphatase
Reaction: a [protein]-Nω-phospho-L-arginine + H2O = a [protein]-L-arginine + phosphate
Other name(s): YwlE
Systematic name: [protein]-Nω-phospho-L-arginine phosphohydrolase
Comments: The enzyme, characterized from Gram-positive bacteria, hydrolyses the phosphoramidate (P-N) bond of Nω-phospho-L-arginine residues in proteins and peptides that were phosphorylated by EC 2.7.14.1, protein-arginine-kinase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Fuhrmann, J., Mierzwa, B., Trentini, D.B., Spiess, S., Lehner, A., Charpentier, E. and Clausen, T. Structural basis for recognizing phosphoarginine and evolving residue-specific protein phosphatases in gram-positive bacteria. Cell Rep 3 (2013) 1832–1839. [PMID: 23770242]
2.  Trentini, D.B., Fuhrmann, J., Mechtler, K. and Clausen, T. Chasing phosphoarginine proteins: development of a selective enrichment method using a phosphatase trap. LID - mcp.O113.035790 [pii. Mol. Cell. Proteomics (2014) . [PMID: 24825175]
3.  Elsholz, A.K., Turgay, K., Michalik, S., Hessling, B., Gronau, K., Oertel, D., Mader, U., Bernhardt, J., Becher, D., Hecker, M. and Gerth, U. Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis. Proc. Natl. Acad. Sci. USA 109 (2012) 7451–7456. [PMID: 22517742]
[EC 3.9.1.2 created 2014]
 
 


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