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. 2014 Jan 13;7(2):184–191. doi: 10.1111/1751-7915.12107

Table 1.

The half-saturation (Michaelis) coefficient (Km), catalytic rate constant (kcat) and catalytic efficiency (kcat/Km) values for the purified CN1E1 esterase for representative, structurally diverse esters. Three independent experiments at 40°C and pH 8.0 (5 mM EPPS buffer) were performed for each parameter, and the data are shown with the standard deviation. The parameters were determined using conditions and methods described previously (Alcaide et al., 2013)

Substrate Km (mM) kcat (s-−1) kcat/Km (s−1 M−1)
pNP-acetate 0.19 ± 0.01 7.52 ± 0.21 39 867
Methyl phenanthrene-9-carboxylate 0.53 ± 0.03 4.76 ± 0.29 8 947
Naphthalene carboxylic acid methyl ester 0.71 ± 0.06 5.82 ± 0.24 8 156
Tri-O-acetyl-D-glucal 1.08 ± 0.05 7.81 ± 0.47 7 237
Phenyl acetate 0.94 ± 0.05 5.75 ± 0.40 6 096
Benzoic acid, 4-formyl-, phenylmethyl ester 0.64 ± 0.06 3.61 ± 0.17 5 626
Protocatechuic acid ethyl ester 1.14 ± 0.06 5.49 ± 0.33 4 798
2,5-Dihydroxycinnamic acid methyl ester 1.06 ± 0.06 5.07 ± 0.17 4 790
Butyl acetate 2.10 ± 0.17 8.76 ± 0.48 4 167
Anthracene-2-carboxylic acid methyl ester 1.47 ± 0.05 5.59 ± 0.20 3 802
Methyl phenanthrene-3-carboxylate 1.60 ± 0.09 4.85 ± 0.18 3 022
Dimethyl phthalate 1.59 ± 0.10 4.75 ± 0.17 2 998
Methyl bromoacetate 1.70 ± 0.09 4.01 ± 0.14 2 358
Triacetin 1.64 ± 0.08 1.82 ± 0.10 1 109