Inhibition of thymidylate synthase by pyridoxal phosphate |
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Authors: | S C Chen H H Daron J L Aull |
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Institution: | Department of Chemistry, Auburn University, AL 36849. |
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Abstract: | 1. Pyridoxal phosphate (PLP) reversibly inhibited thymidylate synthase from Lactobacillus casei with a KI of 0.6-0.9 microM. 2. The inhibition was competitive with dUMP and noncompetitive with 5,10-methylenetetrahydrofolate which is consistent with an ordered addition of substrates. 3. The spectrum of PLP was altered by the addition of thymidylate synthase. The spectral changes suggest formation of a thiohemiacetal with an enzyme sulfhydryl group rather than Schiff base formation with a lysine side chain. |
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