Archaea / 2015 / Article / Tab 1

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].

SubstrateStructure Kcat [s−1] Km [mM]Kcat/Km [s−1M−1]

-(R)-valerolactone6.23 ± 0.424.56 ± 0.511327.1 ± 61.3
-(S)-valerolactone2.68 ± 0.001.95 ± 0.181379.95 ± 110.67
-(R)-caprolactone3.04 ± 0.010.55 ± 0.025563.72 ± 140.96
-(S)-caprolactone1.89 ± 0.110.75 ± 0.042531.22 ± 298.99
Whiskey lactone4.20 ± 0.060.93 ± 0.074538.63 ± 402.78
-Butyrolactone2.79 ± 0.0711.57 ± 0.58241.7 ± 11.18
pNP-acetate1.66 ± 0.348.19 ± 1.10201.74 ± 20.48
Methyl-paraoxon1.25 ± 0.402.79 ± 0.7442.58 ± 50.14

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