TY  - JOUR
AU  - Schulte, Marianne
AU  - Stoldt, Matthias
AU  - Neudecker, Philipp
AU  - Pietruszka, Jӧrg
AU  - Willbold, Dieter
AU  - Panwalkar, Vineet
TI  - $^{1}$H, $^{13}$C, and $^{15}$N backbone and sidechain resonance assignments of a monomeric variant of E. coli deoxyribose-5-phosphate aldolase
JO  - Biomolecular NMR assignments
VL  - 11
IS  - 2
SN  - 1874-270X
CY  - Dordrecht [u.a.]
PB  - Springer Netherlands
M1  - FZJ-2017-05307
SP  - 197-201
PY  - 2017
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:28560616
UR  - <Go to ISI:>//WOS:000410473300015
DO  - DOI:10.1007/s12104-017-9747-6
UR  - https://juser.fz-juelich.de/record/836184
ER  -