Table 1 Substrate specificity and kinetic constants of LacH
From: Biochemical characterization of an enantioselective esterase from Brevundimonas sp. LY-2
Substrate | Specific activity (μmol min−1 mg−1) | k cat (s−1) | K m (mM) | k cat/K m (s−1 mM−1) |
|---|---|---|---|---|
Lactofen | 2.97 ± 0.61 | 0.87 ± 0.09 | 0.067 ± 0.002 | 12.9 |
p-Nitrophenyl acetate | 118 ± 5.3 | 8.39 ± 0.28 | 0.147 ± 0.008 | 50.1 |
p-Nitrophenyl butyrate | 88.1 ± 3.2 | 7.48 ± 0.45 | 0.185 ± 0.009 | 40.4 |
p-Nitrophenyl caproate | 15.8 ± 1.2 | 3.47 ± 0.13 | 0.208 ± 0.012 | 16.7 |
p-Nitrophenyl caprylate | 4.90 ± 0.18 | 0.767 ± 0.06 | 0.335 ± 0.016 | 2.29 |
p-Nitrophenyl laurate | ND | ND | ND | ND |