%0 Journal Article
%A Schulte, Marianne
%A Stoldt, Matthias
%A Neudecker, Philipp
%A Pietruszka, Jӧrg
%A Willbold, Dieter
%A Panwalkar, Vineet
%T $^{1}$H, $^{13}$C, and $^{15}$N backbone and sidechain resonance assignments of a monomeric variant of E. coli deoxyribose-5-phosphate aldolase
%J Biomolecular NMR assignments
%V 11
%N 2
%@ 1874-270X
%C Dordrecht [u.a.]
%I Springer Netherlands
%M FZJ-2017-05307
%P 197-201
%D 2017
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:28560616
%U <Go to ISI:>//WOS:000410473300015
%R 10.1007/s12104-017-9747-6
%U https://juser.fz-juelich.de/record/836184