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000836184 1001_ $$0P:(DE-Juel1)159365$$aSchulte, Marianne$$b0
000836184 245__ $$a$^{1}$H, $^{13}$C, and $^{15}$N backbone and sidechain resonance assignments of a monomeric variant of E. coli deoxyribose-5-phosphate aldolase
000836184 260__ $$aDordrecht [u.a.]$$bSpringer Netherlands$$c2017
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000836184 520__ $$aDeoxyribose-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.
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000836184 7001_ $$0P:(DE-Juel1)132023$$aStoldt, Matthias$$b1
000836184 7001_ $$0P:(DE-Juel1)144510$$aNeudecker, Philipp$$b2
000836184 7001_ $$0P:(DE-HGF)0$$aPietruszka, Jӧrg$$b3
000836184 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b4
000836184 7001_ $$0P:(DE-Juel1)157799$$aPanwalkar, Vineet$$b5$$eCorresponding author$$ufzj
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