3.9.1.2	C14S	mutation of auxiliary cysteine residue present in the active site, significant resuction in kcat value	728854	
3.9.1.2	C7S	structure in complex with phosphate shows the formation of a covalent phospho-Ser7 adduct indicating that the crystallized mutant mimics the phospho-enzyme intermediate of the dephosphorylation reaction	729550	
3.9.1.2	C9A	substrate-trapping mutant, retains binding affinity toward arginine-phosphorylated proteins but cannot hydrolyze the captured substrates. Mutant C9A stably binds to arginine-phosphorylated proteins	-, 730385	
3.9.1.2	C9S	mutation of active site cysteine, complete loss of activity	728854	
3.9.1.2	D118A	complete loss of activity	729550	
3.9.1.2	F120A	60fold reduction of specific activity	729550	
3.9.1.2	T11I	18fold reduction of specific activity with phospho-arginine substrates, marked increasing in the activity toward phospho-tyrosine substrates	729550	
3.9.1.2	T11V	18fold reduction of specific activity with phospho-arginine substrates, marked increasing in the activity toward phospho-tyrosine substrates	729550