Mutations at the putative active cavity of styrene monooxygenase: Enhanced activity and reversed enantioselectivity

Lin, Hui; Tang, Danling; Ahmed, Abeer Ahmed Qaed; Liu, Yan; Wu, Zhong‐Liu

doi:10.1016/j.jbiotec.2012.06.028

Cited by 28 publications

(21 citation statements)

References 36 publications

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“…The specific epoxidation activity of the most active mutant S96A toward styrene and trans-beta-methylstyrene are 2.6 and 2.3-fold of the wild type, respectively. In addition, the Y73V mutant showed an unexpected reversal of enantiomeric preference toward 1-phenylcyclohexene [136]. A similar approach has led to the identification of mutant L45A which exhibits an altered substrate preference toward the bulkier substrate alpha-ethylstyrene rather than styrene [139].…”

Section: Protein Engineering Of Smosmentioning

confidence: 91%

Biocatalytic Epoxidation for Green Synthesis

Lin

Liu

et al. 2016

Green Biocatalysis

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Section: Protein Engineering Of Smosmentioning

confidence: 91%

Biocatalytic Epoxidation for Green Synthesis

Lin

Liu

et al. 2016

Green Biocatalysis

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“…The specific epoxidation activity of the most active mutant S96A toward styrene and trans-β-methylstyrene are 2.6-and 2.3-fold of the wild-type, respectively. In addition, the Y73V mutant showed an unexpected reversal of enantiomeric preference toward 1-phenylcyclohexene (Lin et al 2012). Sequence alignment shows that all SMOs originating from the genus Pseudomonas share the same amino acid residues at positions 73 and 96.…”

Section: Protein Engineering Of Smomentioning

confidence: 96%

“…Sequence alignment shows that all SMOs originating from the genus Pseudomonas share the same amino acid residues at positions 73 and 96. However, self-sufficient one-component StyA2B from R. opacus 1CP has Ile and Ala at the corresponding positions, respectively (Tischler et al 2012), but whether they would indicate higher activity in StyA2B is currently unknown (Lin et al 2012).…”

Section: Protein Engineering Of Smomentioning

confidence: 99%

Asymmetric bio-epoxidation catalyzed with the styrene monooxygenase from Pseudomonas sp. LQ26

Liu

2016

Bioresour. Bioprocess.

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Styrene monooxygenases (SMOs) can catalyze the asymmetric epoxidation of alkenes to obtain optically active epoxides. This account describes a series of work of our group on the isolation, application, and improvement of an SMO from Pseudomonas sp. LQ26. The strain was isolated from an active sludge sample based on indigo-forming capacity. Then the gene encoding SMO was expressed in Escherichia coli, and the whole cells were applied in biocatalytic reactions. The substrate spectrum of SMO was successfully expanded from conjugated styrene derivatives to non-conjugated alkenes, especially α-substituted secondary allylic alcohols, affording enantiopure epoxides. Most significantly, cascade reactions involving ketoreductase and SMO were designed, which resulted in glycidol derivatives or epoxy ketones with excellent enantio-and diastereo-selectivity using α,β-unsaturated ketones as the substrates. In addition, mutants of SMO with altered substrate preference and enhanced activity were constructed, which indicated great potential of SMO for further improvement.

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“…By a similar rational design approach, a different set of mutations was found to exhibit increased epoxidation activity toward styrene and trans -β-methyl styrene compared with the wild-type enzyme. Interestingly, one of these mutants showed reversed enantiomeric preference toward 1-phenylcyclohexene (Lin et al, 2012) (Table 2). …”

Section: Epoxidationsmentioning

confidence: 99%

Flavoprotein monooxygenases for oxidative biocatalysis: recombinant expression in microbial hosts and applications

2014

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External flavoprotein monooxygenases comprise a group of flavin-dependent oxidoreductases that catalyze the insertion of one atom of molecular oxygen into an organic substrate and the second atom is reduced to water. These enzymes are involved in a great number of metabolic pathways both in prokaryotes and eukaryotes. Flavoprotein monooxygenases have attracted the attention of researchers for several decades and the advent of recombinant DNA technology caused a great progress in the field. These enzymes are subjected to detailed biochemical and structural characterization and some of them are also regarded as appealing oxidative biocatalysts for the production of fine chemicals and valuable intermediates toward active pharmaceutical ingredients due to their high chemo-, stereo-, and regioselectivity. Here, we review the most representative reactions catalyzed both in vivo and in vitro by prototype flavoprotein monooxygenases, highlighting the strategies employed to produce them recombinantly, to enhance the yield of soluble proteins, and to improve cofactor regeneration in order to obtain versatile biocatalysts. Although we describe the most outstanding features of flavoprotein monooxygenases, we mainly focus on enzymes that were cloned, expressed and used for biocatalysis during the last years.

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Mutations at the putative active cavity of styrene monooxygenase: Enhanced activity and reversed enantioselectivity

Cited by 28 publications

References 36 publications

Biocatalytic Epoxidation for Green Synthesis

Biocatalytic Epoxidation for Green Synthesis

Asymmetric bio-epoxidation catalyzed with the styrene monooxygenase from Pseudomonas sp. LQ26

Flavoprotein monooxygenases for oxidative biocatalysis: recombinant expression in microbial hosts and applications

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