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KMID : 0380219930260040304
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Journal of Biochemistry and Molecular Biology
1993 Volume.26 No. 4 p.304 ~ p.307
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Characterization of Thymidylate Synthase from Pseudomonas sp. KL-9
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In-Young Kwak and Jong-Soo Lee
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Abstract
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Thymidylate synthase has been isolated from MTX-resistant strains of Pseudomonas sp. KL-9, using a procedure that involves fractionation with ammonium sulfate, filtration through Sephadex G-150, and chromatography on CM-Sephadex. The specific activity of enzyme was 6.4imes10-3U/mg and the overall yield was about 15.3%. This enzyme showed a high substrate specificity on dUMP and THF, and required 2-mercaptoethanol and Mg2+. In tris-acetate buffers, the enzyme displayed pH optimum at 6.5 when dUMP was the substrate. The optimal temperature was 40circC Km values for 5,10-methylenetetrahydrofolate and dUMP were 6.9imes10-7M and 6.6imes10-8M, respectively, which were lower values than the case of L. casei TS.
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