Table 2 Kinetic constant of MTG mutants for the GDH-coupled enzyme assay.
From: Introduction of multiple disulfide bonds increases the thermostability of transglutaminase
| Â | Km | Vmax | kcat | kcat/Km |
|---|---|---|---|---|
mM | µmol/min/mg | s− 1 | M− 1s− 1 | |
WT | 1.7 ± 0.4 | 1.0 ± 0.1 | 0.7 ± 0 | 409 ± 69 |
A81C/V311C | 1.0 ± 0 | 0.9 ± 0 | 0.5 ± 0 | 537 ± 7 |
E93C/V112C | 2.0 ± 0.2 | 1.0 ± 0 | 0.6 ± 0 | 302 ± 21 |
A106C/D213C | 1.8 ± 0.2 | 1.0 ± 0.1 | 0.6 ± 0 | 360 ± 28 |
E107C/Y217C | 1.8 ± 0 | 0.9 ± 0 | 0.5 ± 0 | 294 ± 4 |
A160C/G228C | 1.9 ± 0.1 | 0.9 ± 0 | 0.6 ± 0 | 292 ± 16 |
D3C/G283C | 1.4 ± 0.2 | 0.9 ± 0 | 0.5 ± 0 | 382 ± 26 |
D3C/G283C/A81C/V311C | 0.8 ± 0.1 | 0.8 ± 0 | 0.5 ± 0 | 659 ± 29 |
D3C/G283C/E93C/V112C | 1.8 ± 0.1 | 1.1 ± 0 | 0.7 ± 0 | 385 ± 24 |
D3C/G283C/A106C/D213C | 1.5 ± 0.1 | 1.1 ± 0 | 0.7 ± 0 | 466 ± 24 |
D3C/G283C/E107C/Y217C | 1.5 ± 0 | 1.0 ± 0 | 0.6 ± 0 | 424 ± 8 |
D3C/G283C/A160C/G228C | 1.4 ± 0.1 | 1.0 ± 0 | 0.6 ± 0 | 438 ± 36 |
