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Table 2 Kinetic parameters of wild-type and mutant mPlg*

From: Purification and characterization of mutant miniPlasmin for thrombolytic therapy

mPlm Active μM in 0.5 μM Vmax (μM/Min) Km (μM) Kcat (Min-1) Kcat/Km Kcat/Km Ratio
      (μM-1Min-1)  
01_K698P 0.00375 11 ± 0.5 2145.3 ± 145.5 2933 1.37 0.29
02_WT 0.1265 207 ± 4.9 347 ± 25 1636 4.72 1
03_K698L 0.0685 126 ± 6.8 2459 ± 201 1839 0.75 0.16
04_K698F 0.124 97 ± 4.6 439 ± 59 782 1.78 0.38
05_K698D 0.046 17 ± 1 587 ± 83 370 0.63 0.13
06_K698W 0.0065 72 ± 8 9686 ± 1222 11077 1.14 0.24
07_K698T 0.007 24 ± 1 4107 ± 221 3429 0.83 0.18
08_K698N 0.1625 224 ± 4.4 811 ± 35 1378 1.7 0.36
09_K698I 0.399 152 ± 6.6 1587 ± 118 381 0.24 0.05
10_K698Q 0.129 213 ± 6.5 1406 ± 76 1651 1.17 0.25
11_K698E 0.1905 62 ± 2.8 2411 ± 162 325 0.13 0.03
12_K698V 0.154 202 ± 5.6 1609 ± 77 1312 0.82 0.17
13_K698G 0.108 11 ± 1.4 617 ± 181 102 0.17 0.03
14_K698M 0.127 221 ± 5.6 1664 ± 71 1740 1.05 0.22
15_K698Y 0.3545 33 ± 1.9 2451 ± 209 93 0.04 0.01
16_K698S 0.1405 39 ± 1.3 1776 ± 96 278 0.16 0.03
17_K698A 0.046 11 ± 0.7 885 ± 111 239 0.27 0.06
  1. * Column 1 in Table 2 shows different mutants (WT: wild-type). Column 2 shows the active enzyme calculated from active site titration, which is an indication of either refolding efficiency or stability of the active zymogen. The concentration of the active enzyme was used to calculate Kcat. Columns 3-7 show the measured and calculated kinetic parameters; column 7 shows the ratio of the catalytic efficiency of different mutants compared with the wild-type, which is set to 1.