Characterization of two styrene monooxygenases from marine microbes

Pu, Wei; Cui, Can; Guo, Chao; Wu, Zhong‐Liu

doi:10.1016/j.enzmictec.2018.02.001

Cited by 25 publications

(19 citation statements)

References 51 publications

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“…References of GEMs showing activity in the indigo-blue screening are given in blue. Enzymes that were previously mentioned in literature and in several cases biochemically characterized are underlined (ANS32444, ACR43973, ACR43974 [15][16][17] ; BAL04129, BAL04132 [27] ; ASR05591 [50] ; WP_039579272 [51] ; AAC23718 [24] ; CAA73790 [52] ; ABB03727 [53] ; ABX24519 [30] ; CAA04000 [54] ; ADE62390 [55] ; GAC06215, WP_027855270 [56] ; ABV24041 [25] ; ADU39063, ADU39062 [13] ; ENW75087 [11] ; ARO76328 [12] ; WP_081399512 [14] ; APT36898 [57] ; KWR77134 [58] ; ABQ12175 [59] ; ABZ79366 [60] ; GAB22407, CAG69430 [61] ). Amino acid sequences were aligned by using the ClustalW algorithm and after phylogenetic analysis, the maximum likelihood tree was constructed applying the MEGAX software with bootstraps of 1,000 replicates.…”

Section: Exploration Of Gemsmentioning

confidence: 99%

Accessing Enantiopure Epoxides and Sulfoxides: Related Flavin‐Dependent Monooxygenases Provide Reversed Enantioselectivity

et al. 2019

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Enantiopure organic compounds are of major importance for the chemical and pharmaceutical industry. Flavin‐dependent group E monooxygenases, composed of monooxygenase and reductase, are known to perform epoxidation of substituted alkenes as well as sulfoxidation in a regio‐ and enantioselective fashion. Group E is divided into styrene monooxygenases (SMO) and indole monooxygenases (IMO). Hitherto mainly SMOs have been characterized. In this study, we assayed 31 monooxygenases from both types, while 23 of which showed activity. They almost exclusively produced (S)‐styrene oxide at high enantiomeric excess with maximum activities of 0.73 μmol min−1 mg−1 (kcat=0.54 s−1). In case of sulfoxidation, we found that the enantioselectivity is contrary between both types. IMOs preferably produce the (S)‐enantiomer while SMOs have a tendency to produce the (R)‐enantiomer. Sequence analysis and molecular docking of substrates allowed identifying fingerprint motives: SMO N46‐V48‐H50‐Y73‐H76‐S96 and IMO S46‐Q48‐M50‐V/I73‐I76‐A96. These form an essential part of the active site while the loop (AS44‐51) interacts with the co‐substrate and other amino acids direct the substrate. The motives clearly distinguish group E monooxygenases and define the enantioselectivity and thus direct biotechnological applications. Two‐hour biotransformations with several sulfides in conjunction with upscale experiments (10 and 100 mg scale) resulted in the identification of promising candidates for the realization of biocatalytic processes.

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Section: Exploration Of Gemsmentioning

confidence: 99%

Accessing Enantiopure Epoxides and Sulfoxides: Related Flavin‐Dependent Monooxygenases Provide Reversed Enantioselectivity

et al. 2019

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“…epoxidation; however, no E values were reported for the allylic alcohol tested. [83] Using a reconstructed ancestral protein from six known SMO enzyme sequences, Chen used genome mining to identify a new monooxygenase from Herbaspirillum huttiense (HhMo) able to catalyse the epoxidation of non-conjugated terminal alkenes. [84] Excellent enantioselectivities were achieved (>99% ee for all examples) and far superior results were obtained by comparison with traditional chemical methods such as the Sharpless epoxidation (Scheme 13.c).…”

Section: Minireview 10mentioning

confidence: 99%

Enzymatic Kinetic Resolution by Addition of Oxygen

2020

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Kinetic resolution using biocatalysis has proven to be an excellent complementary technique to traditional asymmetric catalysis for the production of enantioenriched compounds. Resolution using oxidative enzymes produces valuable oxygenated structures for use in synthetic route development. This Minireview focuses on enzymes which catalyse the insertion of an oxygen atom into the substrate and, in so doing, can achieve oxidative kinetic resolution. The Baeyer-Villiger rearrangement, epoxidation, and hydroxylation are included, and biological advancements in enzyme development, and applications of these key enantioenriched intermediates in natural product synthesis are discussed. Scheme 1-Representative early examples of enzymatic OKR. Lucy Harwood received her MSci degree in Chemistry from Queen's University, Belfast completing her final year research project on the use of sigmatropic rearrangements in synthesis in the group of Prof. P. Stevenson. She is currently conducting her doctoral studies at the University of Oxford in the groups of Prof. J. Robertson and Prof. L.-L. Wong developing mutant cytochrome P450s as general oxidation catalysts.

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“…Another interesting styrene monooxygenases are PaSMO and MlSMO. PaSMO is an SMO isolated from Paraglaciecola agarilytica NO 2 (previously Glaciecola agarilytica), an agar-digesting marine bacterium isolated from marine sediment, and MlSMO is an SMO isolated from Marinobacterium litorale DSM 23545, which is example of a mesophile bacteria isolated from surface seawater [92].…”

Section: Styrene Monooxygenasementioning

confidence: 99%

“…The second FAD-binding motif contains the sequence GDX6P (residues 294-302 in MlSMO, residues 292-300 in PaSMO), where the highly conserved Asp moiety connectswith the O3' of the ribose moiety of FAD. The DG sequence is highly conserved among all flavoproteins with hydroxylase activity but only Gly is conservative in StyA (MlSMO residue 171, PaSMO residue 169) [92].…”

Section: Styrene Monooxygenasementioning

confidence: 99%

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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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Characterization of two styrene monooxygenases from marine microbes

Cited by 25 publications

References 51 publications

Accessing Enantiopure Epoxides and Sulfoxides: Related Flavin‐Dependent Monooxygenases Provide Reversed Enantioselectivity

Accessing Enantiopure Epoxides and Sulfoxides: Related Flavin‐Dependent Monooxygenases Provide Reversed Enantioselectivity

Enzymatic Kinetic Resolution by Addition of Oxygen

Biotechnological Methods of Sulfoxidation: Yesterday, Today, Tomorrow

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