3.4.14.4	C113S	mutation of the cysteine residue	707596	
3.4.14.4	C130S	mutant, only existence of dimeric form	707596	
3.4.14.4	C130S	the mutant exhibits comparable enzymatic activity to the wild type protein	-, 698782	
3.4.14.4	C147A	activity similar to wild type	649555	
3.4.14.4	C176A	25-35% of wild type activity, resistant against p-chloro-mercuri-benzoate and N-ethylmaleimide	649555	
3.4.14.4	C176E	no enzymic activity	649555	
3.4.14.4	C176G	no enzymic activity	649555	
3.4.14.4	C19A	activity similar to wild type	649555	
3.4.14.4	C450S	residues Gly383 and Glu320 form significantly less hydrogen bonds with substrate Arg-Arg-2-naphthylamide than in the wild type enzyme	754693	
3.4.14.4	C509A	activity similar to wild type	649555	
3.4.14.4	C518S	mutation of the cysteine residue	707596	
3.4.14.4	C519A	activity similar to wild type	649555	
3.4.14.4	C626S	mutation of the cysteine residue	707596	
3.4.14.4	C639S	mutant, resistance against p-hydroxy-mercuribenzoate	707596	
3.4.14.4	C654A	activity similar to wild type	649555	
3.4.14.4	C701A	activity similar to wild type	649555	
3.4.14.4	D372A	residue Asp372 plays a crucial role in the large scale interdomain closure. During the MD simulation time, the variant remains more open than the wild type protein. Apparently, Ala is not as efficient as Asp in establishing the interdomain interactions	732223	
3.4.14.4	D496G	mutation in S2 subsite, mutant has lost selectivity due to the increase of the Km value. Mutant shows significantly decreased binding of peptides with N-terminal arginine, and of tynorphin	731407	
3.4.14.4	G313A	mutation detected in human cancer, strong decrease in activity. Mutation significantly increases the enzyme flexibility, particularly that of the binding site including the H450ELLGH455 motif, and influences the substrate interactions with the catalytic His568	755384	
3.4.14.4	G313W	mutation detected in human cancer, almost abolishes activity	755384	
3.4.14.4	H450Y	no activity	36186	
3.4.14.4	H455Y	no activity	36186	
3.4.14.4	H578D	mutation 122fold lowers the catalytic efficiency for Arg-Arg 2-naphthylamide hydrolysis, and 14fold decreases affinity for hydroxamate inhibitor Tyr-Phe-NHOH	732012	
3.4.14.4	K638L	mutation slightly increases the specificity constant for Arg-Arg 2-naphthylamide hydrolysis. The affinity for Tyr-Phe-NHOH, and activity for the substrates with uncharged P2 side chains such as Ala-Ala-, Ala-Arg- and Phe-Arg 2-naphthylamide are dramatically reduced	732012	
3.4.14.4	Leu453del	activity of mutant Cu(II)-del-DPP III, in which Leu453 is deleted from the metal-binding motif, is only 1-2% of the enzyme activity of del-DPP. The EPR spectra of Cu(II) del-DPP III do not change in the presence of excess Lys-Ala-beta-naphthylamide. The deletion of Leu453 from the HELLGH motif of rat DPP III leads to a complete loss of flexibility in the ligand geometry around the cupric ions	731219	
3.4.14.4	additional information	design of recombinant enzymes withh binding of Ets-1/Elk-1 proteins to binding motifs, increased enzyme expression	708494	
3.4.14.4	additional information	DPPIII6His, construct with hexahistidine	707596	
3.4.14.4	Q451A	no activity	36186	
3.4.14.4	Q451D	no activity	36186	
3.4.14.4	Q508A	no activity	36186	
3.4.14.4	R510K	mutation detected in human cancer, substitution mildly decreases enzyme activity for Arg-Arg-2-naphtylamide substrate	755384	
3.4.14.4	R510Q	mutation detected in human cancer, strong decrease in activity	755384	
3.4.14.4	R510W	mutation detected in human cancer, almost abolishes activity. Mutation significantly increases the enzyme flexibility, particularly that of the binding site including the H450ELLGH455 motif, and influences the substrate interactions with the catalytic His568	755384	
3.4.14.4	R582Q	mutant exhibits an order of magnitude higher activity with all four dipeptide derivatives examined, compared to the wild type, due to a change in the H-bond networking in the R582Q variant active-site region	732012	
3.4.14.4	S504G	mutation in S2 subsite, mutant does not show decreased binding of peptides with N-terminal arginine	731407	
3.4.14.4	W300F	mutant with slight increase in activity compared to wild-type enzyme	707660	
3.4.14.4	W300L	mutant with higher activity compared to wild-type enzyme	707660	
3.4.14.4	Y318F	the potential functional role of the well-conserved tyrosine 318 residue in the active center of human DPP III is investigated	683209	
3.4.14.4	Y395F	the potential functional role of the well-conserved tyrosine 395 residue in the active center of human DPP III is investigated	683209	
3.4.14.4	Y644F	the potential functional role of the well-conserved tyrosine 644 residue in the active center of human DPP III is investigated	683209