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Title 

Expression and characterization of a novel 2-deoxyribose-5-phosphate aldolase from Haemophilus influenzae Rd KW20

Authors 

Mi-Hee WooMin Soo KimN ChungJoong Su Kim

Publisher 

Korean Society for Applied Biological Chemisty

Issue Date 

2014

Citation 

Journal of Korean Society for Applied Biological Chemistry, vol. 57, no. 5, pp. 655-660

Keywords 

2-deoxyribose-5-phosphate aldolaseHaemophilus influenzaestatin intermediates synthesis

Abstract 

A codon-optimized 2-deoxy?ibose-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°C, respectively. Additionally, the recombinant enzyme retained stability up to temperatures below 50°C. Maximal enzyme activity was observed in presence of 300 mM of acetaldehyde. The apparent Km and Vmax of purified enzyme towards 2-deoxyribose-5-phosphate were 0.14 mM and 70.42 μmol min?1 mg?1 and towards 2-deoxy-D-ribose were 24.77 mM and 1.94 μmol 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.

ISSN 

1738-2203

Link 

http://dx.doi.org/10.1007/s13765-014-4231-9

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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