ArticleJournal of industrial microbiology & biotechnology2013
Characterization and application of a newly synthesized 2-deoxyribose-5-phosphate aldolase.
Article in Journal of industrial microbiology & biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 18 citations in OpenAlex.
- Characterization of 2-deoxyribose-5-phosphate aldolase from Bacillus altitudinis JYY-02.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- Rational engineering of 2-deoxyribose-5-phosphate aldolases for the biosynthesis of (The Journal of biological chemistry · 2020Article
- 2-Deoxy-D-ribose-5-phosphate aldolase (DERA): applications and modifications.Applied microbiology and biotechnology · 2018Review
- A Nuclease fromFrontiers in cellular and infection microbiology · 2017Article
- Expression, characterization, and improvement of a newly cloned halohydrin dehalogenase from Agrobacterium tumefaciens and its application in production of epichlorohydrin.Journal of industrial microbiology & biotechnology · 2014Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
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Abstract
A codon-optimized 2-deoxyribose-5-phosphate aldolase (DERA) gene was newly synthesized and expressed in Escherichia coli to investigate its biochemical properties and applications in synthesis of statin intermediates. The expressed DERA was purified and characterized using 2-deoxyribose-5-phosphate as the substrate. The specific activity of recombinant DERA was 1.8 U/mg. The optimum pH and temperature for DERA activity were pH 7.0 and 35 °C, respectively. The recombinant DERA was stable at pH 4.0-7.0 and at temperatures below 50 °C. The enzyme activity was inhibited by 1 mM of Ni(2+), Ba(2+) and Fe(2+). The apparent K (m) and V (max) values of purified enzyme for 2-deoxyribose-5-phosphate were 0.038 mM and 2.9 μmol min(-1) mg(-1), for 2-deoxyribose were 0.033 mM and 2.59 μmol min(-1) mg(-1), respectively, which revealed that the enzyme had similar catalytic efficiency towards phosphorylated and non-phosphorylated substrates. To synthesize statin intermediates, the bioconversion process for production of (3R, 5S)-6-chloro-2,4,6-trideoxyhexose from chloroacetaldehyde and acetaldehyde by the recombinant DERA was developed and a conversion of 94.4 % was achieved. This recombinant DERA could be a potential candidate for application in production of (3R, 5S)-6-chloro-2,4,6-trideoxyhexose.
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