Home > Publications database > $^{1}$H, $^{13}$C, and $^{15}$N backbone and sidechain resonance assignments of a monomeric variant of E. coli deoxyribose-5-phosphate aldolase > print

001     836184
005     20210129230915.0
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100 1 _ |a Schulte, Marianne
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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
260 _ _ |a Dordrecht [u.a.]
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520 _ _ |a 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.
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700 1 _ |a Stoldt, Matthias
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700 1 _ |a Neudecker, Philipp
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700 1 _ |a Pietruszka, Jӧrg
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700 1 _ |a Willbold, Dieter
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700 1 _ |a Panwalkar, Vineet
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