1H, 13C, and 15N backbone and sidechain resonance assignments of a monomeric variant of E. coli deoxyribose-5-phosphate aldolase.

doi:10.1007/s12104-017-9747-6

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Article

1H, 13C, and 15N backbone and sidechain resonance assignments of a monomeric variant of E. coli deoxyribose-5-phosphate aldolase.

Biomolecular NMR assignments - 1 Oct 2017

Schulte Marianne, Stoldt Matthias, Neudecker Philipp, Pietruszka Jӧrg, Willbold Dieter, Panwalkar Vineet

Abstract excerpt

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...

Topics

Aldehyde-Lyases
Aldehydes
Animals
Escherichia coli
Mutant Proteins
Mutation
Nuclear Magnetic Resonance, Biomolecular

Source

Open in PubMed

Identifiers

PMID: 28560616
DOI: 10.1007/s12104-017-9747-6

Genes

DERA

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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