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Figure 8 | Theoretical Biology and Medical Modelling

Figure 8

From: The allosteric modulation of lipases and its possible biological relevance

Figure 8

Simulated reaction courses using a constant lipase activity a [14]; The rate constants k1 to k8 are defined in Figure 3; a, c, e: Amount of compounds 3, 4 and 5 (n [%]); b, d, f: Enantiomeric excess of (S)-4 (% ee); a, b: non-enantioselective transformation of (S)-4 and (R)-4 into 5 (a = 0.0008); k1 = 17, k2 = 1, k3 = 9, k4 = 9, k5 = 17·10-6, k6 = 1·10-6, k7 = 9·10-6, k8 = 9·10-6; c, d: inhibited transformation of (S)-4 and (R)-4 into 5 (a = 0.0004); k1 = 17, k2 = 1, k3 = 0.009, k4 = 0.009, k5 = 17·10-6, k6 = 1·10-6, k7 = 0.009·10-6, k8 = 0.009·10-6; e, f: non-competitive, since compounds 4 and 5 do not bind to the enzyme (a = 0.02); k1 = 17, k2 = 1.

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