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. 2022 Jun 9;23(12):6438. doi: 10.3390/ijms23126438

Table 3.

Inhibition studies of the chimeric species A1 and A2 of human arginase type I.

Substrate Inhibitor Inhibition Type Kis (mM)
WT-arginase Arginine Guanidine Competitive 56 ± 4
Chimera A1 Arginine graphic file with name ijms-23-06438-i001.jpg Competitive 38 ± 6
Chimera A2 Agmatine Competitive 40 ± 6
WT-arginase Arginine Agmatine Competitive 42 ± 5
Chimera A1 Arginine graphic file with name ijms-23-06438-i002.jpg Competitive 27 ± 2
WT-arginase Arginine Ornithine Competitive 2 ± 0.5
Chimera A1 Arginine graphic file with name ijms-23-06438-i003.jpg Competitive 60 ± 2
Chimera A2 Agmatine Arginine Competitive 9 ± 3
graphic file with name ijms-23-06438-i004.jpg

The values of the kinetic parameters indicated in this table correspond to the results of two experiments performed in duplicate and the standard deviations were not greater than 5%. Chimeric species: A1 (I129T/N130Y/131A mutations); A2 (I129T/N130Y/T131A-∆P132-T134).