3.4.22.70	C184A	catalytically inactive	717705	
3.4.22.70	C184A	mutant enzyme can not cleave the LPXTG motif	647382	
3.4.22.70	C184A	site-directed mutagenesis	731485	
3.4.22.70	C184Hcy	site-directed mutagenesis, generation of a sortase mutant with Cys184 replaced by homocysteine (Hcy). Mutant Hcy-sortase is a poor catalyst with less than 1% of wild-type activity. The sensitivity of the active site nucleophiles towards an alkylation reagent correlates with the pKa values of the mutated residues	731485	
3.4.22.70	C184S	2700fold decrease in kcat/Km compared to wild-type value	678296	
3.4.22.70	C184Sec	site-directed mutagenesis, generation of a sortase mutant with Cys184 replaced by selenocysteine (Sec). Mutant Sec-sortase shows a moderate 2-3fold reduction in catalytic activity. The sensitivity of the active site nucleophiles towards an alkylation reagent correlates with the pKa values of the mutated residues. The pH-profile of mutant Sec-sortase is shifted to more acidic conditions when compared to the wild-type enzyme	731485	
3.4.22.70	D170A	Tm is 1.7°C higher than the Tm-value of wild-type enzyme. No change in kcat/Km compared to wild-type value	680902	
3.4.22.70	D170A	turnover-number for o-aminobenzoyl-LPETG-2,4-dinitrophenyl is nearly identical to wild-type value	665718	
3.4.22.70	D185A 1.3	fold decrease in kcat/Km compared to wild-type value	678296	
3.4.22.70	D186A	1.8fold decrease in kcat/Km compared to wild-type value	678296