A study of substrate specificity of toluene dioxygenase in processing aromatic compounds containing benzylic and/or remote chiral centers

Abstract

A series of substituted arenes containing remote chiral centers were screened as substrates for toluene dioxygenase (TDO). The absolute stereochemistry of the new metabolites was determined by chemical and spectroscopic correlation with synthetic standards. There was no evidence for kinetic resolution ; enantiomers were indiscriminately processed by the enzyme to diastereomeric pairs, which were separable upon derivatization. Some of these new metabolites are useful as synthons for morphine synthesis. Full experimental details are reported for those new compounds stable to isolation and for derivatives of those that are unstable.

Permissivity of the biphenyl-specific aerobic bacterial metabolic pathway towards analogues with various steric requirements

“…NMR data have been presented for the DDs of cyclohexylbenzene and diphenylmethane. They appear to be consistent with our results; however, no assignments for the observed signals were given in the previous report (Bui et al, 2001). For the DD of diphenylacetylene, the only analytical data given were the electronic absorption spectrum (Grund, 1995).…”

“…1). DDs of the same regiospecificity have been reported for cyclohexylbenzene and diphenylmethane, formed by a recombinant strain that synthesized the toluene dioxygenase from Pseudomonas putida F1 (Bui et al, 2001), for diphenylmethane, formed by purified dioxygenases of strain LB400 and of Pandoraea pnomenusa B356 (Pham & Sylvestre, 2013), for cis-stilbene, formed by the mutant TTC1 of the naphthalene degrader Pseudomonas fluorescens N3 (Di Gennaro et al, 1997), and for diphenylacetylene, formed by Pseudomonas sp. strain 73-4 (Grund, 1995).…”

Production of (R)‐1‐phenylethanols through bioreduction of acetophenones by a new fungus isolate Trichothecium roseum

“…[1][2][3][4][5] For example, enantiopure (R)-1-phenylethanol (2a) is an important chiral building block for pharmaceuticals, agrochemicals, and natural products. [6][7][8][9][10] For economic and environmental reasons, biocatalysis has recently gained increasing importance for the preparation of enantiopure alcohols from prochiral ketones. For this purpose, ketoreductases have been shown to be unique biocatalysts in the preparation of enantiopure alcohols from prochiral ketones.…”

The enzymatic basis for pesticide bioremediation

“…This multi-component enzyme not only has extremely broad substrate specifi city but also acts as a dioxygenase or monooxygenase. TOD acts as a dioxygenase against a range of compounds including monocyclic aromatics, fused aromatics, linked aromatics and aliphatic olefi ns [31,32]. TOD also acts as a monooxygenase on monocyclic aromatics, aliphatic olefi ns and other miscellaneous substrates [33,34].…”