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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The interaction of pteroylpolyglutamates with calf thymus thymidylate synthase.

Calf thymus thymidylate synthase was purified to homogeneity using a pteroyltetraglutamyllysine Sepharose affinity column. Inhibition of the purified enzyme by folate or methotrexate was enhanced by addition of gamma-Glu residues. Tetrahydrofolate, tetrahydropteroyltriglutamate and tetrahydropteroylheptaglutamate, all having the natural configuration at C-6, all showed similar Km values near 15 microM. Thus, although calf thymus thymidylate synthase showed a higher affinity for pteroylpolyglutamates than pteroylmonoglutamate, this was not reflected in lowered Km values with the corresponding tetrahydropteroylpolyglutamate substrates.[1]

References

  1. The interaction of pteroylpolyglutamates with calf thymus thymidylate synthase. Dwivedi, C.M., Kisliuk, R.L., Baugh, C.M. Adv. Exp. Med. Biol. (1983) [Pubmed]
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