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Correction for light absorption in fluorescence studies of protein-ligand interactions.
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Human thymidylate synthase is in the closed conformation when complexed with dUMP and raltitrexed, an antifolate drug.
TLDR
The crystal structure of the complex between recombinant human TS, dUMP, and raltitrexed has been determined and the enzyme is in the closed conformation and a covalent bond between the catalytic Cys 195 and dUMP is present in both subunits.
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Immobilized Biochemicals and Affinity Chromatography
TLDR
Two approaches are proposed for the Preparation of Spacer Containing Derivatives and for Specific Isolation of Peptides for Immobilized Enzymes.
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Folylpolyglutamates as substrates and inhibitors of folate-dependent enzymes.
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Cation binding and thermostability of FTHFS monovalent cation binding sites and thermostability of N10-formyltetrahydrofolate synthetase from Moorella thermoacetica.
TLDR
Glu98 is a crucial residue in the interaction of monovalent cations with FTHFS, confirming that the removal of the unbalanced, buried charge of Glu98 stabilizes the enzyme.
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Dihydrofolate reductase from amethopterin-resistant Lactobacillus casei.
The complete amino acid sequence of dihydrofolate reductase from an amethopterin-resistant strain of Lactobacillus casei has been determined by sequence analysis of peptides produced by cleavage with…
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Interaction of dihydrofolate reductase from amethopterin-resistant Lactobacillus casei with Cibacron Blue, Blue Dextran, and Affi-Gel Blue.
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Structural characterization of selenosubtilisin by selenium-77 NMR spectroscopy
The semisynthetic selenoenzyme selenosubtilisin catalyzes the reduction of alkyl hydroperoxides with concomitant oxidation of 3-carboxy-4-nitrobenzenethiol. To gain insight into the mechanism of this…
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Structure of Human Thymidylate Synthase Suggests Advantages of Chemotherapy with Noncompetitive Inhibitors*
TLDR
TS inhibition via stabilization of the inactive conformation should lead to less resistance than is observed with presently used drugs, which are analogs of its substrates, dUMP and CH2H4folate, and bind in the active site, promoting the active conformation.
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Purification and characterization of selenomethionyl thymidylate synthase from Escherichia coli: comparison with the wild-type enzyme.
TLDR
Comparisons of the properties of selenomethionyl thymidylate synthase isolated from Escherichia coli DL41 and wild-type (wt) enzyme obtained from E. coli Rue10 show no significant difference in conformation between the SeMet enzyme and the wt enzyme.
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