This title appears in the Scientific Report :
2016
Please use the identifier:
http://dx.doi.org/10.1371/journal.pone.0156525 in citations.
Please use the identifier: http://hdl.handle.net/2128/13559 in citations.
Redesigning Aldolase Stereoselectivity by Homologous Grafting
Redesigning Aldolase Stereoselectivity by Homologous Grafting
The 2-deoxy-d-ribose-5-phosphate aldolase (DERA) offers access to highly desirable building blocks for organic synthesis by catalyzing a stereoselective C-C bond formation between acetaldehyde and certain electrophilic aldehydes. DERA´s potential is particularly highlighted by the ability to catalyz...
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Personal Name(s): | Bisterfeld, Carolin |
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Classen, Thomas / Küberl, Irene / Henßen, Birgit / Metz, Alexander / Gohlke, Holger / Pietruszka, Jörg (Corresponding author) | |
Contributing Institute: |
Institut für Bioorganische Chemie (HHUD); IBOC Biotechnologie; IBG-1 |
Published in: | PLoS one, 11 (2016) 6, S. e0156525 - |
Imprint: |
Lawrence, Kan.
PLoS
2016
|
DOI: |
10.1371/journal.pone.0156525 |
Document Type: |
Journal Article |
Research Program: |
Biotechnology |
Link: |
OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://hdl.handle.net/2128/13559 in citations.
The 2-deoxy-d-ribose-5-phosphate aldolase (DERA) offers access to highly desirable building blocks for organic synthesis by catalyzing a stereoselective C-C bond formation between acetaldehyde and certain electrophilic aldehydes. DERA´s potential is particularly highlighted by the ability to catalyze sequential, highly enantioselective aldol reactions. However, its synthetic use is limited by the absence of an enantiocomplementary enzyme. Here, we introduce the concept of homologous grafting to identify stereoselectivity-determining amino acid positions in DERA. We identified such positions by structural analysis of the homologous aldolases 2-keto-3-deoxy-6-phosphogluconate aldolase (KDPG) and the enantiocomplementary enzyme 2-keto-3-deoxy-6-phosphogalactonate aldolase (KDPGal). Mutation of these positions led to a slightly inversed enantiopreference of both aldolases to the same extent. By transferring these sequence motifs onto DERA we achieved the intended change in enantioselectivity. |