ExplorEnz: EC 3.9.1.2

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3.9.1.2

Accepted name:

protein arginine phosphatase

Reaction:

a [protein]-N^ω-phospho-L-arginine + H₂O = a [protein]-L-arginine + phosphate

Other name(s):

YwlE

Systematic name:

[protein]-N^ω-phospho-L-arginine phosphohydrolase

Comments:

The enzyme, characterized from Gram-positive bacteria, hydrolyses the phosphoramidate (P-N) bond of N^ω-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, GENE, KEGG, MetaCyc, PDB

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. [DOI] [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) . [DOI] [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. [DOI] [PMID: 22517742]

[EC 3.9.1.2 created 2014]