Optimized oxidoreductases for medium and large scale industrial biotransformations
Total records:
126
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[ 2019 ]
Linde D, Ayuso-Fernández I, Ruiz-Dueñas FJ, Martínez AT Different fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan
Arch. Biochem. Biophys., 668: 23-28
[ 2019 ]
Serrano A, Sancho F, Viña-Gonzalez J, Carro J, Alcalde M, Guallar V, Martínez AT Switching the substrate preference of fungal aryl-alcohol oxidase: towards stereoselective oxidation of secondary benzyl alcohols
Catal. Sci. Technol., doi: 10.1039/C8CY02447B
[ 2019 ]
Viña-Gonzalez J, Jimenez-Lalana D, Sancho F, Serrano A, Martínez AT, Guallar V, Alcalde M Structure‐Guided Evolution of Aryl Alcohol Oxidase from Pleurotus eryngii for the Selective Oxidation of Secondary Benzyl Alcohols
Adv. Synth. Catal., 361: 2514-2525
[ 2018 ]
Carro J, Fernandez-Fueyo E, Fernández-Alonso C, Cañada J, Ullrich R, Hofrichter M, Alcalde M, Ferreira P, Martínez AT Self-sustained enzymatic cascade for the production of 2,5-furandicarboxylic acid from 5-methoxymethylfurfural
Biotechnol. Biofuels, 11: 86-96
[ 2018 ]
Carro J, Ferreira P, Martínez AT, Gadda G Stepwise Hydrogen Atom and Proton Transfers in Dioxygen Reduction by Aryl-Alcohol Oxidase
Biochemistry, doi: 10.1021/acs.biochem.8b00106
[ 2018 ]
Ewing TA, Kühn J, Segarra S, Tortajada M, Zuhse R, van Berkel WJ Multigram Scale Enzymatic Synthesis of (R)‐1‐(4′‐Hydroxyphenyl)ethanol Using Vanillyl Alcohol Oxidase
Adv. Synth. Catal., 360: 2370-2376
year2016
Asymmetric sulfoxidation by engineering the heme pocket of a dye-decolorizing peroxidase: An experimental and computational study
Linde D, Cañellas M, Coscolín C, Davó-Siguero I, Romero A, Lucas F, Ruiz-Dueñas FJ, Guallar V, Martínez AT
Catal. Sci. Technol., 6: 6277-6285
The so-called dye-decolorizing peroxidases (DyPs) constitute a new family of proteins exhibiting remarkable stability. With the aim of providing them new catalytic activities of biotechnological interest, the heme pocket of one of the few DyPs fully characterized to date (from the fungus Auricularia auricula-judae) was redesigned based on the crystal structure available, and its potential for asymmetric sulfoxidation was evaluated. Chiral sulfoxides are important targets in organic synthesis and enzyme catalysis, due to a variety of applications. Interestingly, one of the DyP variants, F359G, is highly stereoselective sulfoxidizing methyl-phenyl sulfide and methyl-p-tolyl sulfide (95-99% conversion, with up to 99% excess of the S enantiomer in short reaction times) while the parent DyP has no sulfoxidation activity, and the L357G variant produces both the R and S enantiomers. The two variants were crystallized and their crystal structures were used in molecular simulations to provide a rational explanation for the new catalytic activities. Protein energy landscape exploration (PELE) showed more favorable protein-substrate catalytic complexes for the above variants, with a considerable number of structures near the oxygen atom of the activated heme, which incorporates to the substrates as shown in 18O-labeling experiments, and improved affinity with respect to the parent enzyme, explaining their sulfoxidation activity. Additional quantum mechanics/molecular mechanics (QM/MM) calculations were performed to elucidate the high stereoselectivity observed for the F359G variant, which correlated with higher reactivity on the substrate molecules adopting pro-S poses at the active site. Similar computational analyses can help to introduce/improve (stereoselective) sulfoxidation activity in related hemeproteins.
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[ industrialoxidoreductases ]. Optimized oxidoreductases for medium and large scale industrial biotransformations. This project has received funding from the European Union’s Seventh Framework Programme for research, technological development and demonstration under Grant Agreement nº: FP7-KBBE-2013-7-613549. © indox 2013. Developed by
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