Please use this identifier to cite or link to this item: https://doi.org/10.1038/sj.jim.7000240
Title: Purification and characterization of recombinant malate synthase enzymes from streptomyces coelicolor a3(2) and s. clavuligerus Nrrl3585
Authors: Loke, P. 
Goh, L.-L.
Seng Soh, B. 
Yeow, P.
Sim, T.-S. 
Keywords: Acetyl-CoA
Enzyme activity
Glyoxylate
GST
Malate synthase
Protein expression
Streptomyces coelicolor, S. clavuligerus
Issue Date: 2002
Citation: Loke, P., Goh, L.-L., Seng Soh, B., Yeow, P., Sim, T.-S. (2002). Purification and characterization of recombinant malate synthase enzymes from streptomyces coelicolor a3(2) and s. clavuligerus Nrrl3585. Journal of Industrial Microbiology and Biotechnology 28 (4) : 239-243. ScholarBank@NUS Repository. https://doi.org/10.1038/sj.jim.7000240
Abstract: Malate synthases (MS) from Streptomyces coelicolor A3(2) and S. clavuligerus NRRL3585 were cloned by polymerase chain reaction into a glutathione S-transferase (GST) fusion expression vector and heterologously expressed in Escherichia coli. The fusion GST-MS construct improved the soluble expression of MS by approximately 10-fold compared to the soluble expression of nonfusion MS. With the significant improvement in levels of soluble MS, purification and subsequent cleavage of recombinant MS from GST were facilitated in this study. Using purified enzymes, optimized parameters, which achieved maximal specific activity, were established in the enzymatic assay for streptomycete MS. The average purified specific activities of S. coelicolorand S. clavuligerus MS were 26199 and 11821 nmol/mg min, respectively. Furthermore, enzymatic analysis revealed that the two streptomycete MS displayed a similar Km value for acetyl-CoA, but S. coelicolor MS had a Km value for glyoxylate that is approximately sixfold higher than S. clavuligerus MS.
Source Title: Journal of Industrial Microbiology and Biotechnology
URI: http://scholarbank.nus.edu.sg/handle/10635/130342
ISSN: 13675435
DOI: 10.1038/sj.jim.7000240
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