Enantioselectivity of Enzymes

Hollmann, Frank; Otten, Linda G.

doi:10.1002/9780470048672.wecb150

Cited by 4 publications

(2 citation statements)

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“…Because of the cooperation of the catalytic centre and the second coordination sphere, a native metalloenzyme can achieve biological transformations with remarkable efficiency and enantioselectivity under mild conditions in vivo 1 2 . Over the years, significant efforts have been dedicated to the biomimetic study of metalloenzymes to understand their structures and functions and design analogues to mimic the native enzymes’ structures and functions 3 .…”

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confidence: 99%

Enantioselective Hydrolysis of Amino Acid Esters Promoted by Bis(β-cyclodextrin) Copper Complexes

Xue

Zhao

et al. 2016

Sci Rep

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It is challenging to create artificial catalysts that approach enzymes with regard to catalytic efficiency and selectivity. The enantioselective catalysis ranks the privileged characteristic of enzymatic transformations. Here, we report two pyridine-linked bis(β-cyclodextrin) (bisCD) copper(II) complexes that enantioselectively hydrolyse chiral esters. Hydrolytic kinetic resolution of three pairs of amino acid ester enantiomers (S1–S3) at neutral pH indicated that the “back-to-back” bisCD complex CuL1 favoured higher catalytic efficiency and more pronounced enantioselectivity than the “face-to-face” complex CuL2. The best enantioselectivity was observed for N-Boc-phenylalanine 4-nitrophenyl ester (S2) enantiomers promoted by CuL1, which exhibited an enantiomer selectivity of 15.7. We observed preferential hydrolysis of L-S2 by CuL1, even in racemic S2, through chiral high-performance liquid chromatography (HPLC). We demonstrated that the enantioselective hydrolysis was related to the cooperative roles of the intramolecular flanking chiral CD cavities with the coordinated copper ion, according to the results of electrospray ionization mass spectrometry (ESI-MS), inhibition experiments, rotating-frame nuclear Overhauser effect spectroscopy (ROESY), and theoretical calculations. Although the catalytic parameters lag behind the level of enzymatic transformation, this study confirms the cooperative effect of the first and second coordination spheres of artificial catalysts in enantioselectivity and provides hints that may guide future explorations of enzyme mimics.

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confidence: 99%

Enantioselective Hydrolysis of Amino Acid Esters Promoted by Bis(β-cyclodextrin) Copper Complexes

Xue

Zhao

et al. 2016

Sci Rep

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“…Native metalloenzymes possess impressive catalytic efficiency and exquisite substrate specificity, regio-and enantio-selectivity, owing to the cooperation of the catalytic centre and the second coordination sphere [1,2]. For example, the (S)-2-hydroxypropylphosphonate ((S)-2-HPP) epoxidase (HppE) reaction course is governed by the stereochemistry of substrates, as the substrate enantiomers proceeded totally different reactions [3,4]; ␣-chymotrypsin catalyzes the hydrolysis of peptide bonds at the carboxyl side of specific amino acid residues in proteins, and has marked enantioselectivity in hydrolyzing certain amino acid esters [5].…”

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confidence: 99%