Enthalpic and entropic contributions to lipase enantioselectivity

Overbeeke, P.L.Antoine; Orrenius, S; Jongejan, Jaap A.; Duine, Johannis A.

doi:10.1016/s0009-3084(98)00031-0

Cited by 24 publications

(10 citation statements)

References 77 publications

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“…(3) (Overbeeke et al, 1998). The observed Arrhenius plots are essentially linear, justifying the assumption that ⌬C P,R-S is zero over the temperature trajectory used in our experiments, allowing us to calculate As a result the change of the difference in Gibbs free energy of activation for the two enantiomers, ⌬⌬G R-S # , is much smaller.…”

Section: Resultssupporting

confidence: 60%

See 1 more Smart Citation

Solvent effect on lipase enantioselectivity. Evidence for the presence of two thermodynamic states

Heijnen

2000

Biotechnol. Bioeng.

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Section: Resultssupporting

confidence: 60%

“…(6A) and (6B) as described before (Overbeeke et al, 1998; for explanation of symbols, see legend to Fig. 6):…”

Section: Discussionmentioning

confidence: 99%

Solvent effect on lipase enantioselectivity. Evidence for the presence of two thermodynamic states

Heijnen

2000

Biotechnol. Bioeng.

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“…The thermodynamic analysis has been proposed to investigate effects of solvent type and mixture, acyl donor and acceptor, lipase type, and mutant on the temperature dependence of E-value in lipase-catalyzed kinetic resolutions (Antoine Overbeeks et al, 1998;Ema et al, 2003;LopezSerrano et al, 2001;Ottosson et al, , 2002. The difference in activation free energy DDG (¼ DG f ÀDG s ) for the transient states of fast-reacting enantiomer, usually (S)-thioester, and the slow-reacting enantiomer can be separated into the differences in activation enthalpy (DDH) and activation entropy (DDS).…”

Section: Thermodynamic Analysismentioning

confidence: 99%

Partially purifiedCarica papayalipase: a versatile biocatalyst for the hydrolytic resolution of (R,S)-2-arylpropionic thioesters in water-saturated organic solvents

Ng¹,

Tsai²

2005

Biotechnol. Bioeng.

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With the hydrolytic resolution of (R,S)-naproxen 2,2,2-trifluoroethyl thioesters in water-saturated isooctane as a model system, improvements of the specific lipase activity and thermal stability were found when a crude Carica papaya lipase (CPL) was partially purified and employed as the biocatalyst. The partially purified Carica papaya lipase (PCPL) was furthermore explored as an effective enantioselective biocatalyst for the hydrolytic resolution of (R,S)-profen thioesters in water-saturated organic solvents. The kinetic analysis in water-saturated isooctane indicated that both acyl donor and acyl acceptor have profound influences on the lipase activity, E-value, and enantioselectivity. Inversion of the enantioselectivity from (S)- to (R)-thioester was found for (R,S)-fenoprofen and (R,S)-ketoprofen thioesters that contained a bulky substituent at the meta-position of 2-phenyl moiety of the acyl part. Kinetic constants for the acylation step were furthermore estimated for elucidating the kinetic data and postulating an active site model. The thermodynamic analysis indicated that the enantiomer discrimination was driven by the difference of activation enthalpy (DeltaDeltaH) and that of activation entropy (DeltaDeltaS), yet the latter was dominated for most of the reacting systems. The postulated active site model was supported from the variation of DeltaDeltaH and DeltaDeltaS with the acyl moiety, in which a good linear enthalpy-entropy compensation relationship was also illustrated. A comparison of the performances between Candida rugosa lipase (CRL) and PCPL indicated that PCPL was superior to CRL in terms of the better thermal stability, similar or better lipase activity for the fast-reacting substrate, time-course-stability, and lower enzyme cost.

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“…The whole catalytic process consists of four procedures, and has two tetrahedral intermediates (TIs) (Kraut, 1977). Based on this catalytic mechanism, Overbeeke et al (1998) revealed a close relationship (Eq. 1) between the enzyme enantioselectivity that is usually represented by the catalytic enantiomeric ratio (E) and the activation free energy difference (DDG 6 ¼ ) between substrate enantiomers ( Fig.…”

Section: Introductionmentioning

confidence: 91%

“…Usually, the enzyme that presents higher enantioselectivity has the preferred substrate enantiomer bound in tighter way, thus, results in bigger entropy lose (Bocola et al, 2003). It has been revealed that the entropy difference between enantiomers (DDS 6 ¼ ) has enormous contribution to the reaction DDG 6 ¼ value (Ottosson et al, 2001(Ottosson et al, , 2002Overbeeke et al, 1998).…”

Section: Prediction Errormentioning

confidence: 99%

Prediction of the enantioselectivity of lipases and esterases by molecular docking method with modified force field parameters

Ji¹,

Tang²,

Yu³

2009

Biotech & Bioengineering

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In the work, molecular docking method was applied to extensively predict the enantioselectivity of lipases and esterases. A ligand library consisted of 69 chiral substrates was docked to four lipases and two esterases to set up the prediction model. During the docking process, necessary modification was carried out on van de Waals and hydrogen bond parameters of enzyme/substrate pair so that the ligands were able to adopt productive geometry in the enzymes. The docking results correctly indicated the enantiopreference for 91% (63/69) of docking pairs and the docking energy difference between substrate enantiomers (Delta Delta G(docking)) was significantly (correlation coefficient = 0.72, P < 0.05) correlated with the activation free energy difference (Delta Delta G( not equal)) that was quantitatively correlated with enantioselectivity of the enzymes. The prediction method was further validated by docking with another 12 enzyme/substrate pairs. Moreover, the prediction error was susceptible to the size of groups bonded to substrate's chiral center and expected Delta Delta G( not equal) values but was not related to the substrate type and reaction medium. The possible reasons of observed error were discussed. It is demonstrated that the docking method has great application potential in high performance prediction of enzyme enantioselectivity.

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Enthalpic and entropic contributions to lipase enantioselectivity

Cited by 24 publications

References 77 publications

Solvent effect on lipase enantioselectivity. Evidence for the presence of two thermodynamic states

Solvent effect on lipase enantioselectivity. Evidence for the presence of two thermodynamic states

Partially purifiedCarica papayalipase: a versatile biocatalyst for the hydrolytic resolution of (R,S)-2-arylpropionic thioesters in water-saturated organic solvents

Prediction of the enantioselectivity of lipases and esterases by molecular docking method with modified force field parameters

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