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A 1 H n.m.r. study of the role of the glutamate moiety in the binding of methotrexate to Lactobacillus casei dihydrofolate reductase
Author(s) -
Antonjuk David J.,
Birdsall Berry,
Cheung H.T. Andrew,
Clore G. Marius,
Feeney James,
Gronenborn Angela,
Roberts Gordon C.K.,
Tran Trung Q.
Publication year - 1984
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.1984.tb10080.x
Subject(s) - lactobacillus casei , dihydrofolate reductase , carboxylate , chemistry , methotrexate , amide , moiety , stereochemistry , enzyme , biochemistry , biology , immunology , fermentation
1 The binding of a series of amide derivatives of methotrexate to Lactobacillus casei dihydrofolate reductase has been studied by inhibition constant measurements and by 1 H n.m.r. spectroscopy. 2 Amide modification of the α‐carboxylate of methotrexate was found to prevent interaction of the γ‐carboxylate with the imidazole of His 28. 3 Estimates of the contributions to the binding energy from the α‐carboxylate‐Arg 57 and γ‐carboxylate‐His 28 interactions have been made from a combination of inhibition and n.m.r. data.