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@ARTICLE{Schulte:836184,
author = {Schulte, Marianne and Stoldt, Matthias and Neudecker,
Philipp and Pietruszka, Jӧrg and Willbold, Dieter and
Panwalkar, Vineet},
title = {$^{1}${H}, $^{13}${C}, and $^{15}${N} backbone and
sidechain resonance assignments of a monomeric variant of
{E}. coli deoxyribose-5-phosphate aldolase},
journal = {Biomolecular NMR assignments},
volume = {11},
number = {2},
issn = {1874-270X},
address = {Dordrecht [u.a.]},
publisher = {Springer Netherlands},
reportid = {FZJ-2017-05307},
pages = {197-201},
year = {2017},
abstract = {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.},
cin = {IBOC / IBG-1 / ICS-6},
ddc = {570},
cid = {I:(DE-Juel1)IBOC-20090406 / I:(DE-Juel1)IBG-1-20101118 /
I:(DE-Juel1)ICS-6-20110106},
pnm = {581 - Biotechnology (POF3-581)},
pid = {G:(DE-HGF)POF3-581},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:28560616},
UT = {WOS:000410473300015},
doi = {10.1007/s12104-017-9747-6},
url = {https://juser.fz-juelich.de/record/836184},
}