Table 2 Enzymatic characterization of the AaL enzyme. Related chemical structures of substrates are presented in Table S1.

From: Structural and Biochemical Characterization of AaL, a Quorum Quenching Lactonase with Unusual Kinetic Properties

Substrates

kcat (s −1)

KM (μM)

kcat/KM(M −1 s −1)

C4- AHL (l)*

12.6 ± 0.8

9.4 ± 2.5

(1.3 ± 0.4) × 106

C6- AHL (l)*

14.0 ± 0.4

82.7 ± 11.0

(1.7 ± 0.2) × 105

C10- AHL (l)*

5.2 ± 0.3

57.2 ± 17.4

(9.2 ± 2.8) × 104

3-Oxo-C12-AHL (l) *

4.9 ± 0.3

17.4 ± 4.8

(2.8 ± 0.8) × 105

γ-butyrolactone

23.5 ± 1.7

171.0 ± 36.1

(1.4 ± 0.3) × 105

γ-heptanolide

7.0 ± 0.3

36.9 ± 8.9

(1.9 ± 0.4) × 104

δ-valerolactone

8.4 ± 0.4

18.7 ± 0.4

(4.5 ± 0.9) × 105

δ-decalactone

8.4 ± 0.6

18.5 ± 0.4

(4.5 ± 1.0) × 105

Paraoxon-ethyl

ND

ND

22.9 ± 1.4

  1. Kinetics were measured as quadruplicates, and standard deviation values are given for each parameter. The kinetics were performed in activity buffer (2.5 mM Bicine pH 8.3, 150 mM NaCl, 0.2 mM cresol purple, 0.5% DMSO and with 0.2 mM CoCl2). ND corresponds to not determined values because of too low catalytic rate. *Data from34.
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