This title appears in the Scientific Report :
2017
Please use the identifier:
http://dx.doi.org/10.1007/s12104-017-9747-6 in citations.
$^{1}$H, $^{13}$C, and $^{15}$N backbone and sidechain resonance assignments of a monomeric variant of E. coli deoxyribose-5-phosphate aldolase
$^{1}$H, $^{13}$C, and $^{15}$N backbone and sidechain resonance assignments of a monomeric variant of E. coli deoxyribose-5-phosphate aldolase
Deoxyribose-5-phosphate aldolase (DERA) catalyses the reversible conversion of 2-deoxyribose-5-phosphate (dR5P) into glyceraldehyde-3-phosphate (G3P) and acetaldehyde. For industrial applications, this enzyme is used in organic synthesis for aldol reactions between acetaldehyde as a donor and a wide...
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Personal Name(s): | Schulte, Marianne |
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Stoldt, Matthias / Neudecker, Philipp / Pietruszka, Jӧrg / Willbold, Dieter / Panwalkar, Vineet (Corresponding author) | |
Contributing Institute: |
Strukturbiochemie; ICS-6 Biotechnologie; IBG-1 Institut für Bioorganische Chemie (HHUD); IBOC |
Published in: | Biomolecular NMR assignments, 11 (2017) 2, S. 197-201 |
Imprint: |
Dordrecht [u.a.]
Springer Netherlands
2017
|
DOI: |
10.1007/s12104-017-9747-6 |
PubMed ID: |
28560616 |
Document Type: |
Journal Article |
Research Program: |
Biotechnology |
Publikationsportal JuSER |
Deoxyribose-5-phosphate aldolase (DERA) catalyses the reversible conversion of 2-deoxyribose-5-phosphate (dR5P) into glyceraldehyde-3-phosphate (G3P) and acetaldehyde. For industrial applications, this enzyme is used in organic synthesis for aldol reactions between acetaldehyde as a donor and a wide range of aldehydes as acceptors. Here, we present a near complete set of sequence-specific 1H, 13C and 15N resonance assignments of a 28 kDa monomeric variant of the Escherichia coli DERA. These assignments provide the basis for ongoing structural and dynamic analysis of DERA substrate specificity. |