Side chain oxidation of aromatic compounds by fungi. 7. A rationale for sulfoxidation, benzylic hydroxylation, and olefin oxidation by Mortierella isabellina

Holland, Herbert L.; Allen, Lisa J.; Chernishenko, Michael J.; Dı́ez, Maria Teresa; Kohl, A.; Ozog, John; Gu, Jinjie

doi:10.1016/s1381-1177(97)00015-5

Cited by 31 publications

(6 citation statements)

References 28 publications

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“…Subsequent studies conducted under the guidance of Holland showed that similar sulfides were also oxidized using the strain M. isabellina ATCC 4261 3 (Scheme 1). However, the formation of R-isomers was preferred here [22,23]. Further research has suggested that both strains of Helminthosporium and M. isabellina use other enzymes for the oxidation of sulfides [24].…”

Section: Fungus and Yeastmentioning

confidence: 99%

Biotechnological Methods of Sulfoxidation: Yesterday, Today, Tomorrow

2018

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The production of chiral sulphoxides is an important part of the chemical industry since they have been used not only as pharmaceuticals and pesticides, but also as catalysts or functional materials. The main purpose of this review is to present biotechnological methods for the oxidation of sulfides. The work consists of two parts. In the first part, examples of biosyntransformation of prochiral sulfides using whole cells of bacteria and fungi are discussed. They have more historical significance due to the low predictability of positive results in relation to the workload. In the second part, the main enzymes responsible for sulfoxidation have been characterized such as chloroperoxidase, dioxygenases, cytochrome flavin-dependent monooxygenases, and P450 monooxygenases. Particular emphasis has been placed on the huge variety of cytochrome P450 monooxygenases, and flavin-dependent monooxygenases, which allows for pure sulfoxides enantiomers effectively to be obtained. In the summary, further directions of research on the optimization of enzymatic sulfoxidation are indicated.

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Section: Fungus and Yeastmentioning

confidence: 99%

Biotechnological Methods of Sulfoxidation: Yesterday, Today, Tomorrow

2018

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“…The proposed "cubic model" had been examined for other substrates, demonstrating that the orientation inside the active-site model is dominated by hydrophobic interactions and steric hindrances. Based on the stereochemical outcome of over 90 biooxidations of organic sulfides, Holland et al (1997aHolland et al ( , b, 1999b) elegantly proposed a model which explains the enantioselectivity of the biotransformation depending on the substrate structure and its orientation inside the active site.…”

Section: Oxidation Reactionsmentioning

confidence: 99%

Enzymatic reactions involving the heteroatoms from organic substrates

Netto

Palmeira

Brondani

et al. 2018

An. Acad. Bras. Ciênc.

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Several enzymatic reactions of heteroatom-containing compounds have been explored as unnatural substrates. Considerable advances related to the search for efficient enzymatic systems able to support a broader substrate scope with high catalytic performance are described in the literature. These reports include mainly native and mutated enzymes and whole cells biocatalysis. Herein, we describe the historical background along with the progress of biocatalyzed reactions involving the heteroatom(S, Se, B, P and Si) from hetero-organic substrates.

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“…2, originally developed to account for the substrate and stereoselectivity of benzylic hydroxylation of hydrocarbons by M. isabellina NRRL 1757 (ATCC 42613), was later extended to cover the enantioselective oxidation of aryl and benzyl alkyl sulfides to (R)-sulfoxides. 100 This model can be used to predict the structures of substrates that will be efficiently converted to (R)-sulfoxides by this biocatalyst. These include aryl alkyl sulfides such as p-bromophenyl methyl sulfide (ee >98%) or 3,5-dimethylphenyl methyl sulfide (ee 84%) which optimally occupy the aromatic binding pocket (A), substrates such as phenyl n-propyl sulfide (ee >98%) that fill the aliphatic binding region (B), and substrates such as 34 and 35 with a substituent (O and NH, respectively) that can interact with the polar binding site (P) of the latter region.…”

Section: Mortierella Isabellinamentioning

confidence: 99%

Biotransformation of organic sulfides (1991 to mid 2000)

Holland

2001

Nat. Prod. Rep.

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Covering 1991 to mid 2000. 1 Introduction 1.1 Asymmetric oxidation of sulfides by isolated enzymes 1.1.1 Cyclohexanone monooxygenase 1.1.2 Chloroperoxidase 1.1.3 Other haloperoxidases 1.1.4 Other peroxidases 1.1.5 Dioxygenases 1.1.6 Monooxygenases 1.1.7 Other enzymes 1.2 Asymmetric oxidation of sulfides by whole-cell biocatalysts 1.2.1 Bacteria 1.2.2 Fungi 1.2.3 Yeasts 1.2.4 Other systems 2 Predictive models for biocatalytic sulfoxidation 2.1 Cyclohexanone monooxygenase 2.2 Mortierella isabellina 2.3 Helminthosporium species 2.4 Other systems 3 Applications of biocatalytically-derived chiral sulfoxides 3.1 Chiral synthons 3.2 Chiral targets 4 Other applications of biocatalytic sulfide oxidation 4.1 Biodesulfurisation 4.2 Drug metabolism 4.3 Other applications 5 Conclusions 6 References

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Side chain oxidation of aromatic compounds by fungi. 7. A rationale for sulfoxidation, benzylic hydroxylation, and olefin oxidation by Mortierella isabellina

Cited by 31 publications

References 28 publications

Biotechnological Methods of Sulfoxidation: Yesterday, Today, Tomorrow

Biotechnological Methods of Sulfoxidation: Yesterday, Today, Tomorrow

Enzymatic reactions involving the heteroatoms from organic substrates

Biotransformation of organic sulfides (1991 to mid 2000)

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