Journal Article

FZJ-2017-05307

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png $^{1}$H, $^{13}$C, and $^{15}$N backbone and sidechain resonance assignments of a monomeric variant of E. coli deoxyribose-5-phosphate aldolase

Schulte, M.FZJ* ; Stoldt, M.FZJ* ; Neudecker, P.FZJ* ; Pietruszka, J.FZJ* ; Willbold, D.FZJ* ; Panwalkar, V. (Corresponding author)FZJ*

2017
Springer Netherlands Dordrecht [u.a.]

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Please use a persistent id in citations: doi:10.1007/s12104-017-9747-6

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.

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Contributing Institute(s):

1. Institut für Bioorganische Chemie (HHUD) (IBOC)
2. Biotechnologie (IBG-1)
3. Strukturbiochemie (ICS-6)

Research Program(s):

1. 581 - Biotechnology (POF3-581) (POF3-581)

Appears in the scientific report 2017

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Database coverage:
; BIOSIS Previews ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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