Functionalization and Modification of Hydrocarbon-Like Molecules Guided by Metagenomics: Enzymes Most Requested at the Industrial Scale for Chemical Synthesis as Study Cases

Martínez-Martínez, Mónica; Bargiela, Rafael; Coscolín, Cristina; Navarro-Fernández, José; Golyshin, Peter N.; Ferrer, Manuel

doi:10.1007/978-3-319-31421-1_211-1

Cited by 2 publications

(4 citation statements)

References 64 publications

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“…In an ideal scenario, functional screening with genomics and metagenomics techniques would allow the identification of a new generation of microbial biocatalysts, including ATAs of the class III ω-TAs (3–6). However, extensive bioprospecting by metagenomics was only rarely successful (5), despite the growing number of sequences available in public databases (7).…”

Section: Introductionmentioning

confidence: 99%

Bioprospecting Reveals Class III ω-Transaminases Converting Bulky Ketones and Environmentally Relevant Polyamines

Coscolín

Katzke

García-Moyano

et al. 2019

Appl Environ Microbiol

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Amine transaminases of the class III ω-TAs are key enzymes for modification of chemical building blocks, but finding those capable of converting bulky ketones and (R) amines is still challenging. Here, by an extensive analysis of the substrate spectra of 10 class III ω-TAs, we identified a number of residues playing a role in determining the access and positioning of bulky ketones, bulky amines, and (R)- and (S) amines, as well as of environmentally relevant polyamines, particularly putrescine. The results presented can significantly expand future opportunities for designing (R)-specific class III ω-TAs to convert valuable bulky ketones and amines, as well as for deepening the knowledge into the polyamine catabolic pathways.

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Section: Introductionmentioning

confidence: 99%

Bioprospecting Reveals Class III ω-Transaminases Converting Bulky Ketones and Environmentally Relevant Polyamines

Coscolín

Katzke

García-Moyano

et al. 2019

Appl Environ Microbiol

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“…Promiscuous esterases acting against multiple substrates, while at the same time being enantio-selective, appear to be rare in nature, or at least in the habitats from where the esterases herein described were isolated [5]. As these enzymes are of interest for application purposes [1][2][3][4][5][6]32], protein engineering and rational design may be needed to obtain esterases being promiscuous and selective for industrial applications. We anticipate that the possibility to transform a promiscuous but not selective esterase into an efficient enantio-selective biocatalyst would require less engineering effort because increasing the selectivity for an enantiomer may involve a reduced number of contacts close to the active sites (for a recent example see reference [33]).…”

Section: Discussionmentioning

confidence: 99%

“…Presently, there is a great need for suitable biocatalysts with high process performance as greener alternatives to chemical synthesis [1,2]. It is expected that up to 40% of bulk chemical synthesis processes could be substituted by enzymatic catalysis by 2020 [1].…”

Section: Introductionmentioning

confidence: 99%

“…Promiscuous enzymes are effective for converting multiple substrates, thus, they are industrially relevant [4][5][6]. Enzymes need to also be robust and, preferably, chiral selective to reduce raw material costs in the synthesis of pure chiral compounds [1,2,4,7]. That is, they need to be able to cleave preferentially only one chiral ester when offered a racemic mixture.…”

Section: Introductionmentioning

confidence: 99%

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Relationships between Substrate Promiscuity and Chiral Selectivity of Esterases from Phylogenetically and Environmentally Diverse Microorganisms

et al. 2018

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Substrate specificity and selectivity of a biocatalyst are determined by the protein sequence and structure of its active site. Finding versatile biocatalysts acting against multiple substrates while at the same time being chiral selective is of interest for the pharmaceutical and chemical industry. However, the relationships between these two properties in natural microbial enzymes remain underexplored. Here, we performed an experimental analysis of substrate promiscuity and chiral selectivity in a set of 145 purified esterases from phylogenetically and environmentally diverse microorganisms, which were assayed against 96 diverse esters, 20 of which were enantiomers. Our results revealed a negative correlation between substrate promiscuity and chiral selectivity in the evaluated enzymes. Esterases displaying prominent substrate promiscuity and large catalytic environments are characterized by low chiral selectivity, a feature that has limited commercial value. Although a low level of substrate promiscuity does not guarantee high chiral selectivity, the probability that esterases with smaller active sites possess chiral selectivity factors of interest for industry (>25) is significantly higher than for promiscuous enzymes. Together, the present study unambiguously demonstrates that promiscuous and selective esterases appear to be rare in nature and that substrate promiscuity can be used as an indicator of the chiral selectivity level of esterases, and vice versa.

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Functionalization and Modification of Hydrocarbon-Like Molecules Guided by Metagenomics: Enzymes Most Requested at the Industrial Scale for Chemical Synthesis as Study Cases

Cited by 2 publications

References 64 publications

Bioprospecting Reveals Class III ω-Transaminases Converting Bulky Ketones and Environmentally Relevant Polyamines

Bioprospecting Reveals Class III ω-Transaminases Converting Bulky Ketones and Environmentally Relevant Polyamines

Relationships between Substrate Promiscuity and Chiral Selectivity of Esterases from Phylogenetically and Environmentally Diverse Microorganisms

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