ArticleChemical science2016
Linking coupled motions and entropic effects to the catalytic activity of 2-deoxyribose-5-phosphate aldolase (DERA).
Article in Chemical science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 20 citations in OpenAlex.
- Engineering 2-Deoxy-D-ribose-5-phosphate Aldolase for anti- and syn-Selective Epoxidations of α,β-Unsaturated Aldehydes.Angewandte Chemie (International ed. in English) · 2025Article
- Current state of and need for enzyme engineering of 2-deoxy-D-ribose 5-phosphate aldolases and its impact.Applied microbiology and biotechnology · 2021Review
- Rational engineering of 2-deoxyribose-5-phosphate aldolases for the biosynthesis of (The Journal of biological chemistry · 2020Article
- Conformational dynamics and enzyme evolution.Journal of the Royal Society, Interface · 2018Review
- Conformational Sampling of the Intrinsically Disordered C-Terminal Tail of DERA Is Important for Enzyme Catalysis.ACS catalysis · 2018Article
- Shuffling Active Site Substate Populations Affects Catalytic Activity: The Case of Glucose Oxidase.ACS catalysis · 2017Article
- Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer.Biochemistry · 2016Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
DERA, 2-deoxyribose-5-phosphate aldolase, catalyzes the retro-aldol cleavage of 2-deoxy-ribose-5-phosphate (dR5P) into glyceraldehyde-3-phosphate (G3P) and acetaldehyde in a branch of the pentose phosphate pathway. In addition to the physiological reaction, DERA also catalyzes the reverse addition reaction and, hence, is an interesting candidate for bio-catalysis of carbo-ligation reactions, which are central to synthetic chemistry. An obstacle to overcome for this enzyme to become a truly useful biocatalyst, however, is to relax the very strict dependency of this enzyme on phosphorylated substrates. We have studied herein the role of the non-canonical phosphate-binding site of this enzyme, consisting of Ser
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Registered trials
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