Isoenzymes of Pig‐Liver Esterase Reveal Striking Differences in Enantioselectivities

Hummel, Anke; Brüsehaber, Elke; Böttcher, Dominique; Trauthwein, Harald; Doderer, Kai; Bornscheuer, Uwe T.

doi:10.1002/anie.200703256

Cited by 51 publications

(38 citation statements)

References 15 publications

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“…Interestingly, an inverse enantiopreference of the two PLE isoenzymes was observed in the case of 1c. This demonstrates, as has already been shown before for the resolution of secondary alcohol acetates, [27] how isoenzymes with high sequence similarity can vary in their properties thus broadening the substrate scope. Moreover, the isoenzyme γPLE showed excellent and good enantioselectivity towards compounds 1a and 1c, respectively.…”

Section: Activity Of the Enzymesmentioning

confidence: 52%

“…[19,23] The strains were grown in 400 mL LB liquid media supplemented with the appropriate antibiotics (100 µg mL -1 ) ampicillin for BS2 variants [24] and PestE, [26] additionally 50 µg mL -1 kanamycin for PPE and the PLE variants [27] at 37°C and supplemented with the appropriate inductor to induce esterase production at an optical density of 0.5 at 600 nm. Cultivation continued for 4 h at the appropriate cultivation temperature.…”

Section: Methodsmentioning

confidence: 99%

“…Recombinantly expressed isoenzymes of pig liver esterase (PLE) offer several advantages over the use of the commercially available crude extract, which consists of a mixture of different isoenzymes, such as a higher enantioselectivity, a higher reproducibility, and fewer regulatory issues. [27] The sequences of the two isoenzymes γPLE and PLE5 differ only in 21 amino acids, but this leads to a striking change in enantioselectivity and enantiopreference towards the acetates of secondary alcohols.…”

Section: Introductionmentioning

confidence: 99%

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An Enzymatic Toolbox for the Kinetic Resolution of 2‐(Pyridin‐x‐yl)but‐3‐yn‐2‐ols and Tertiary Cyanohydrins

et al. 2010

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The kinetic resolution of a series of acetates of tertiary alcohols bearing a nitrogen substituent has been studied by using several recombinant carboxyl esterases and variants thereof expressed in E. coli. Most of the enzymes were active in the conversion of these tertiary alcohols and excellent enantioselectivities were achieved in the synthesis of three 2-(pyridin-x-yl)but-3-yn-2-ols with the nitrogen atom in the pyridine ring in the 2Ј-, 3Ј-, and 4Ј-positions. The resolution

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Section: Activity Of the Enzymesmentioning

confidence: 52%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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An Enzymatic Toolbox for the Kinetic Resolution of 2‐(Pyridin‐x‐yl)but‐3‐yn‐2‐ols and Tertiary Cyanohydrins

et al. 2010

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“…They differ by a small number of mutations (Table 1) and were denoted PLE1-5 [12]. PLE1 is identical to the former -PLE, whereas no unique assignment of the former and modifications was possible.…”

Section: Introductionmentioning

confidence: 99%

Simulation on the structure of pig liver esterase

2010

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International audienceA homology model for pig liver esterase was generated on the basis of human carboxyl esterase (hCE) and subjected to extensive molecular dynamics simulations. By virtual mutations the isoenzymes PLE1-6 and APLE were obtained, and the PLE1 trimer was built from the respective model of hCE. Stable structures for all systems were attained after simulations in solution for 12-18 ns, and contact zones between the monomers in the trimer are described. By evaluation of RMSD values of the residues in the monomer a rigid backplane with a number of β-strands and a flexible front part containing several α helices are distinguished. All mutations are concentrated in the soft part, and significant differences in the folding states of the helices were distinguished between the isoenzymes. Substrate access to the active site passes through two helices whose structures are affected by mutations. Variations in substrate specificity between the isoenzymes are ascribed to the structure of the entrance channel rather than to the conformation of the active site itself. The assignment of the residue with a negative side chain stabilizing the histidine protonation in the catalytic triad was revised, being GLU 452 in some isoenzymes rather than GLU 336, which would be the correspondent to most hydrolases. Arguments for this new assignment are given on the basis of simulations and statistics from the 3DM database for hydrolases

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“…54 Os β-hidroxi- Nesta etapa do trabalho foi mostrada a importância da triagem e monitoramento de reações com microrganismos para a seleção de biocatalisadores com a seletividade desejada.…”

Section: Padrão Racêmico 1aunclassified

Biocatálise aplicada à síntese de núcleos <i>β</i>-hidroxi-1,2,3-triazólicos e síntese multienzimática do alcaloide diidropinidina

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Isoenzymes of Pig‐Liver Esterase Reveal Striking Differences in Enantioselectivities

Cited by 51 publications

References 15 publications

An Enzymatic Toolbox for the Kinetic Resolution of 2‐(Pyridin‐x‐yl)but‐3‐yn‐2‐ols and Tertiary Cyanohydrins

An Enzymatic Toolbox for the Kinetic Resolution of 2‐(Pyridin‐x‐yl)but‐3‐yn‐2‐ols and Tertiary Cyanohydrins

Simulation on the structure of pig liver esterase

Biocatálise aplicada à síntese de núcleos <i>β</i>-hidroxi-1,2,3-triazólicos e síntese multienzimática do alcaloide diidropinidina

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Isoenzymes of Pig‐Liver Esterase Reveal Striking Differences in Enantioselectivities

Cited by 51 publications

References 15 publications

An Enzymatic Toolbox for the Kinetic Resolution of 2‐(Pyridin‐x‐yl)but‐3‐yn‐2‐ols and Tertiary Cyanohydrins

An Enzymatic Toolbox for the Kinetic Resolution of 2‐(Pyridin‐x‐yl)but‐3‐yn‐2‐ols and Tertiary Cyanohydrins

Simulation on the structure of pig liver esterase

Biocatálise aplicada à síntese de núcleos <i>&#946;</i>-hidroxi-1,2,3-triazólicos e síntese multienzimática do alcaloide diidropinidina

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Biocatálise aplicada à síntese de núcleos <i>β</i>-hidroxi-1,2,3-triazólicos e síntese multienzimática do alcaloide diidropinidina