This title appears in the Scientific Report :
2017
Please use the identifier:
http://dx.doi.org/10.1016/j.jbiotec.2017.03.024 in citations.
Probing the acetaldehyde-sensitivity of 2-deoxy-ribose-5-phosphate aldolase (DERA) leads to resistant variants
Probing the acetaldehyde-sensitivity of 2-deoxy-ribose-5-phosphate aldolase (DERA) leads to resistant variants
The 2-deoxy-d-ribose-5-phosphate aldolase (DERA) is a synthetically attractive enzyme because of its ability to perform CC-couplings stereoselectively, the enzyme uses acetaldehyde as nucleophile and thus produces true aldols rather than ketols, and may add two acetaldehyde molecules onto one electr...
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Personal Name(s): | Bramski, Julia |
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Dick, Markus / Pietruszka, Jörg / Classen, Thomas (Corresponding author) | |
Contributing Institute: |
Biotechnologie; IBG-1 Institut für Bioorganische Chemie (HHUD); IBOC |
Published in: | Journal of biotechnology, 258 (2017) S. 56-58 |
Imprint: |
Amsterdam [u.a.]
Elsevier Science
2017
|
PubMed ID: |
28347769 |
DOI: |
10.1016/j.jbiotec.2017.03.024 |
Document Type: |
Journal Article |
Research Program: |
Biotechnology |
Publikationsportal JuSER |
The 2-deoxy-d-ribose-5-phosphate aldolase (DERA) is a synthetically attractive enzyme because of its ability to perform CC-couplings stereoselectively, the enzyme uses acetaldehyde as nucleophile and thus produces true aldols rather than ketols, and may add two acetaldehyde molecules onto one electrophile. However, DERA produces crotonaldehyde as side reaction from acetaldehyde which is then an irreversible inhibitor forming a covalent Michael-adduct within the active site in particular with cysteine 47 (Dick et al., 2016). This inhibition can be resolved by mutating C47 to non-nucleophile amino acids. Still, the inhibition is not an on-off-feature and the present mutagenesis study illustrates that there must be a C47-independent inactivation mechanism. As a practical result: The virtually fully resistant mutant C47L was found, which shows no loss in stereoselectivity, − this renders this variant as promising catalyst. |