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Expression and Characterization of a Novel 2-Deoxyribose-5-phosphate Aldolase from Haemophilus influenzae Rd KW20

Authors
Woo, Mi-HeeKim, Min SooChung, NamhyunKim, Joong-Su
Issue Date
10월-2014
Publisher
KOREAN SOC APPLIED BIOLOGICAL CHEMISTRY
Keywords
2-deoxyribose-5-phosphate aldolase; Haemophilus influenzae; statin intermediates synthesis
Citation
JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY, v.57, no.5, pp.655 - 660
Indexed
SCIE
SCOPUS
KCI
Journal Title
JOURNAL OF THE KOREAN SOCIETY FOR APPLIED BIOLOGICAL CHEMISTRY
Volume
57
Number
5
Start Page
655
End Page
660
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/97192
DOI
10.1007/s13765-014-4231-9
ISSN
1738-2203
Abstract
A codon-optimized 2-deoxyribose-5-phosphate aldolase (DERA) gene from Haemophilus influenzae Rd KW20 was synthesized and expressed in Escherichia coli, and the biochemical properties of its product were investigated. DERA was purified using affinity chromatography and characterized using 2-deoxyribose-5-phosphate as the substrate. Specific activity of the recombinant DERA was 34.1 Umg(-1). The pH and temperature optima were 7.5 and 40 degrees C, respectively. Additionally, the recombinant enzyme retained stability up to temperatures below 50 degrees C. Maximal enzyme activity was observed in presence of 300 mM of acetaldehyde. The apparent K-m and V-max of purified enzyme towards 2-deoxyribose-5-phosphate were 0.14 mM and 70.42 fond min(-1) mg(-1) and towards 2-deoxy-D-ribose were 24.77 mM and 1.94 mu mol min(-1) mg(-1), respectively. For synthesis of statin intermediates, the bioconversion process for production of (3R, 5S)-6-chloro-2,4,6-trideoxy-erythro-hexose from chloroacetaldehyde and acetaldehyde using the recombinant DERA was studied and this process took 3 h for maximal conversion. This recombinant DERA could be potentially applied in the production of (3R, 5S)-6-chloro-2,4,6-trideoxy-erythro-hexose.
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