Review Article
Archaeal Enzymes and Applications in Industrial Biocatalysts
Table 1
The kinetic parameters of the activity of the VmutPLL enzyme with different lactone substrates. Taken from Kallnik et al., 2014 [
45].
| Substrate | Structure |
Kcat [s−1] |
Km [mM] | Kcat/Km [s−1M−1] |
| -(R)-valerolactone | | 6.23 ± 0.42 | 4.56 ± 0.51 | 1327.1 ± 61.3 | -(S)-valerolactone | | 2.68 ± 0.00 | 1.95 ± 0.18 | 1379.95 ± 110.67 | -(R)-caprolactone | | 3.04 ± 0.01 | 0.55 ± 0.02 | 5563.72 ± 140.96 | -(S)-caprolactone | | 1.89 ± 0.11 | 0.75 ± 0.04 | 2531.22 ± 298.99 | Whiskey lactone | | 4.20 ± 0.06 | 0.93 ± 0.07 | 4538.63 ± 402.78 | -Butyrolactone | | 2.79 ± 0.07 | 11.57 ± 0.58 | 241.7 ± 11.18 | pNP-acetate | | 1.66 ± 0.34 | 8.19 ± 1.10 | 201.74 ± 20.48 | Methyl-paraoxon | | 1.25 ± 0.40 | 2.79 ± 0.7 | 442.58 ± 50.14 |
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