Synthesis of 10-acetyl-5,8-dideazafolic acid: a potent inhibitor of glycinamide ribonucleotide transformylase.

@article{Caperelli1986SynthesisO1,
  title={Synthesis of 10-acetyl-5,8-dideazafolic acid: a potent inhibitor of glycinamide ribonucleotide transformylase.},
  author={Carol A. Caperelli and James P. Conigliaro},
  journal={Journal of medicinal chemistry},
  year={1986},
  volume={29 10},
  pages={
          2117-9
        }
}
10-Acetyl-5,8-dideazafolic acid has been synthesized in good yield from the parent compound, 5,8-dideazafolic acid. This quinazoline folate analogue showed no activity as a substrate for the folate-requiring de novo purine biosynthetic enzyme glycinamide ribonucleotide transformylase isolated from the murine lymphoma cell line L5178Y, but proved to be a potent competitive inhibitor, Ki = 1.3 microM, of the purified enzyme. 
View on PubMed
doi.org
12 Citations
Methods Citations
2

12 Citations

Carbocyclic glycinamide ribonucleotide is a substrate for glycinamide ribonucleotide transformylase.
Synthesis of analogues of folic acid, aminopterin and methotrexate as antitumour agents.
Stereoselective Synthesis of β-Glycinamide Ribonucleotide
TLDR
A diastereoselective synthesis of the β-anomer of glycinamide ribonucleotide (β-GAR) has been developed and was remarkably resistant to anomerization both in solution and as a solid.
The human glycinamide ribonucleotide transformylase domain: purification, characterization, and kinetic mechanism.
TLDR
The correspondence of data obtained for the glycinamide ribonucleotide transformylase activity of the mammalian trifunctional enzyme indicates that the recombinant enzyme is fully functional.
The human trifunctional enzyme of de novo purine biosynthesis: heterologous expression, purification, and preliminary characterization.
TLDR
The correspondence of data obtained for the glycinamide ribonucleotide transformylase activity of the mammalian trifunctional enzyme indicates that the recombinant enzyme is fully functional.
Human glycinamide ribonucleotide transformylase: active site mutants as mechanistic probes.
TLDR
Differences between human and Escherichia coli GART, previously used as a model for the human enzyme, were evident and inactive mutants were able to bind both substrates, ruling out disrupted formation of the ternary complex as the source of inactivity.
PvdF of pyoverdin biosynthesis is a structurally unique N10-formyltetrahydrofolate-dependent formyltransferase
TLDR
Steady state kinetics revealed a non-hyperbolic rate curve, promoting the hypothesis that PvdF uses a random-sequential mechanism, and favors folate binding over OHOrn.
PvdF of pyoverdin biosynthesis is a structurally unique N10-formyltetrahydrofolate-dependent formyltransferase.
Chapter 14 Anti-neoplastic Agents
A Broad View Of Active Residues That Mediate Catalysis For Ornithine Transcarbamoylase And Glycinamide Ribonucleotide Transformylase
...
...