This title appears in the Scientific Report :
2022
Please use the identifier:
http://hdl.handle.net/2128/32071 in citations.
Please use the identifier: http://dx.doi.org/10.3390/catal12101195 in citations.
Identification and Characterization of the Haloperoxidase VPO-RR from Rhodoplanes roseus by Genome Mining and Structure-Based Catalytic Site Mapping
Identification and Characterization of the Haloperoxidase VPO-RR from Rhodoplanes roseus by Genome Mining and Structure-Based Catalytic Site Mapping
Halogenating enzymes have evolved in considerable mechanistic diversity. The apparent need for secondary metabolism coincides with the current need to introduce halogens in synthetic products. The potential of halogenating enzymes and, especially, vanadate-dependent haloperoxidases has been insuffic...
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Personal Name(s): | Porta, Nicola |
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Fejzagić, Alexander Veljko / Dumschott, Kathryn / Paschold, Beatrix / Usadel, Björn / Pietruszka, Jörg / Classen, Thomas (Corresponding author) / Gohlke, Holger (Corresponding author) | |
Contributing Institute: |
Institut für Bioorganische Chemie (HHUD); IBOC Strukturbiochemie; IBI-7 John von Neumann - Institut für Computing; NIC Jülich Supercomputing Center; JSC Biotechnologie; IBG-1 Bioinformatik; IBG-4 |
Published in: | Catalysts, 12 (2022) 10, S. 1195 - |
Imprint: |
Basel
MDPI
2022
|
DOI: |
10.3390/catal12101195 |
Document Type: |
Journal Article |
Research Program: |
Molecular Information Processing in Cellular Systems Bioeconomy Science Center Forschergruppe Gohlke Domain-Specific Simulation & Data Life Cycle Labs (SDLs) and Research Groups Biological and environmental resources for sustainable use |
Link: |
OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.3390/catal12101195 in citations.
Halogenating enzymes have evolved in considerable mechanistic diversity. The apparent need for secondary metabolism coincides with the current need to introduce halogens in synthetic products. The potential of halogenating enzymes and, especially, vanadate-dependent haloperoxidases has been insufficiently exploited for synthetic purposes. In this work, we identified potential halogenase sequences by screening algal, fungal, and protobacterial sequence databases, structural modeling of putative halogenases, and mapping and comparing active sites. In a final step, individual haloperoxidases were expressed and kinetically characterized. A vanadate-dependent haloperoxidase from Rhodoplanes roseus was heterologously expressible by E. coli and could be purified to homogeneity. The kinetic data revealed a higher turnover number than the known VClPO-CI and no inhibitory effect from bromide, rendering this enzyme a promising biocatalyst. Other predicted haloperoxidases were not expressed successfully yet but these enzymes were predicted to be present in a wide taxonomic variety. |