Resolution of alpha/beta-amino acids by enantioselective penicillin G acylase from Achromobacter sp.
| Authors | |
|---|---|
| Year of publication | 2015 |
| Type | Article in Periodical |
| Magazine / Source | JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC |
| MU Faculty or unit | |
| Citation | |
| Web | http://www.sciencedirect.com/science/article/pii/S1381117715300692 |
| Doi | http://dx.doi.org/10.1016/j.molcatb.2015.09.008 |
| Field | Biochemistry |
| Keywords | Penicillin G acylase; Enantioselectivity; Homologous model; Docking experiments; alpha/beta-amino acid |
| Description | Penicillin G acylases (PGAs) are enantioselective enzymes catalyzing a hydrolysis of stable amide bond in a broad spectrum of substrates. Among them, derivatives of alpha- and beta-amino acids represent a class of compounds with high application potential. PGA(Ec) from Escherichia coil and PGA(A) from Achromobacter sp. CCM 4824 were used to catalyze enantioselective hydrolyses of seven selected N-phenylacetylated alpha/beta-amino acid racemates. The PGA(A) showed higher stereoselectivity for enantiomers of N-PhA-beta-homoleucine, N-PhAc-alpha-tert-leucine and N-PhAc-beta-leucine. To study the mechanism of enantiodiscrimination on molecular level, we have constructed a homology model of PGA(A) that was used in molecular docking experiments with the same substrates. In-silico experiments successfully reproduced the data from experimental enzymatic resolutions confirming validity of employed modeling protocol. We employed this protocol to evaluate enantiopreference of PGA(A) towards seven new substrates with application potential. For five of them, high enantioselectivity of PGA(A) was predicted. |
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