Optimized oxidoreductases for medium and large scale industrial biotransformations
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126
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[ 2016 ]
Kellner H, Pecyna MJ, Buchhaupt M, Ullrich R, Hofrichter M Draft Genome Sequence of the Chloroperoxidase-Producing Fungus Caldariomyces fumago Woronichin DSM1256
Genome Announc., 4
[ 2016 ]
Kracher D, Scheiblbrandner S, Felice AKG, Breslmayr E, Preims M, Ludwicka K, Haltrich D, Eijsink VG, Ludwig R Extracellular electron transfer systems fuel cellulose oxidative degradation
Science, 352: 1098-1101
[ 2016 ]
Linde D, Cañellas M, Coscolín C, Davó-Siguero I, Romero A, Lucas F, Ruiz-Dueñas FJ, Guallar V, Martínez AT Asymmetric sulfoxidation by engineering the heme pocket of a dye-decolorizing peroxidase: An experimental and computational study
Catal. Sci. Technol., 6: 6277-6285
[ 2016 ]
Lourenço A, Rencoret J, Chemetova C, Gominho J, Gutiérrez A, del Río JC, Pereira H Lignin Composition and Structure Differs between Xylem, Phloem and Phellem in Quercus suber L.
Front. Plant Sci., 7: 1612
[ 2016 ]
Lucas F, Babot ED, Cañellas M, del Río JC, Kalum L, Ullrich R, Hofrichter M, Guallar V, Martínez AT, Gutiérrez A Molecular determinants for selective C25-hydroxylation of vitamins D2 and D3 by fungal peroxygenases
Catal. Sci. Technol., 6: 288-295
[ 2016 ]
Martínez AT How to break down crystalline cellulose
Science, 352: 1050-1051
year2016
Molecular determinants for selective C25-hydroxylation of vitamins D2 and D3 by fungal peroxygenases
Lucas F, Babot ED, Cañellas M, del Río JC, Kalum L, Ullrich R, Hofrichter M, Guallar V, Martínez AT, Gutiérrez A
Catal. Sci. Technol., 6: 288-295
Hydroxylation of vitamin D by Agrocybe aegerita and Coprinopsis cinerea peroxygenases was investigated in a combined experimental and computational study. 25-Monohydroxylated vitamins D3 (cholecalciferol) and D2 (ergocalciferol), compounds of high interest in human health and animal feeding, can be obtained through a reaction with both fungal enzymes. Differences in conversion rates, and especially in site selectivity, were observed. To rationalize the results, diffusion of D2 and D3 on the molecular structure of the two enzymes was performed using the PELE software. In good agreement with experimental conversion yields, simulations indicate more favorable energy profiles for the substrates entrance in C. cinerea than for A. aegerita enzyme. On the other hand, GC-MS analyses show that while a full regioselective conversion of D2 and D3 into the active C25 form is catalyzed by C. cinerea peroxygenase, A. aegerita yielded a mixture of the hydroxylated D3 products. From the molecular simulations, relative distance distributions between the haem compound I oxygen atom and H24/H25 atoms (hydrogens on C24 and C25, respectively) were plotted. Results show large populations for O-H25 distances below 3 Amstrong for D2 and D3 in C. cinerea in accordance with the high reactivity observed for this enzyme. In A. aegerita, however, cholecalciferol has similar populations (below 3 Amstrong) for O-H25 and O-H24, which can justify the hydroxylation observed in C24. In the case of ergocalciferol, due to the bulky methyl group in position C24, very few structures are found with O-H24 distances below 3 Amstrong and thus, as expected, the reaction was only observed at the C25 position.
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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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