Multi-Temperature Crystallography of Polyamine Biosynthesis Enzymes Reveals Differing Active Site Conformations at RT than 100K [PDF]
The polyamine biosynthetic pathway synthesizes the polyamines putrescine, spermidine, and spermine from ornithine and S-adenosyl methionine. These polyamines are important molecules in metabolism and are associated with growth and proliferation of cells ...
Jonathan A Clinger
doaj +2 more sources
Discovery of Potent and Selective Inhibitors of Trypanosoma brucei Ornithine Decarboxylase [PDF]
Human African trypanosomiasis, caused by the eukaryotic parasite Trypanosoma brucei, is a serious health problem in much of central Africa. The only validated molecular target for treatment of human African trypanosomiasis is ornithine decarboxylase (ODC), which catalyzes the first step in polyamine metabolism. Here, we describe the use of an enzymatic
David C Smithson +2 more
exaly +3 more sources
Structural and degradative aspects of ornithine decarboxylase antizyme inhibitor 2 [PDF]
Ornithine decarboxylase (ODC) is the key enzyme in the polyamine biosynthetic pathway. ODC levels are controlled by polyamines through the induction of antizymes (AZs), small proteins that inhibit ODC and target it to proteasomal degradation without ...
Bruno Ramos-Molina +7 more
doaj +3 more sources
The remarkable legacy of the K6/ODC mouse: mechanisms of polyamine-promoted tumorigenesis revealed [PDF]
Using the well-studied two-stage model of skin carcinogenesis, the first transgenic mouse with targeted expression of a polyamine metabolic enzyme was generated 30 years ago.
Susan K. Gilmour
doaj +2 more sources
Baicalein, 7,8-Dihydroxyflavone and Myricetin as Potent Inhibitors of Human Ornithine Decarboxylase [PDF]
Background: Human ornithine decarboxylase (ODC) is a well-known oncogene, and the discovery of ODC enzyme inhibitors is a beneficial strategy for cancer therapy and prevention. Methods: We examined the inhibitory effects of a variety of flavone and flavonol derivatives on ODC enzymatic activity, and performed in silico molecular docking of baicalein, 7,
Yi-Liang Liu +2 more
exaly +3 more sources
Design, Synthesis, and Biological Activity of Novel Ornithine Decarboxylase (ODC) Inhibitors. [PDF]
We here describe the design, synthesis, and biological activity of novel ornithine decarboxylase (ODC) inhibitors that show significantly higher potency in vitro than α-difluoromethylornithine (DFMO), a U.S. Food and Drug Administration (FDA) approved drug.
Schultz CR +8 more
europepmc +3 more sources
Ornithine decarboxylase (ODC) catalyzes the first step in the polyamines (PAs) biosynthesis pathway. These biomolecules are polycations that participate in many cellular processes. However, the non-physiological increase of human ODC (HsODC) expression can lead to the accumulation of PAs, and consequently, to the development of various types of cancer.
Samuel Álvarez-Almazán +2 more
exaly +3 more sources
Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor but not an arginine decarboxylase [PDF]
ODC (ornithine decarboxylase), the rate-limiting enzyme in polyamine biosynthesis, is regulated by specific inhibitors, AZs (antizymes), which in turn are inhibited by AZI (AZ inhibitor). We originally identified and cloned the cDNA for a novel human ODC-like protein called ODCp (ODC paralogue).
Kanerva, Kristiina +4 more
openaire +5 more sources
Putrescine is a low-molecular-weight organic compound that is widely found in pickled foods. Although the intake of biogenic amines is beneficial to humans, an excessive intake can cause discomfort.
Zhe Xu +7 more
doaj +1 more source
A macromolecular inhibitor of the antizyme to ornithine decarboxylase [PDF]
A macromolecular factor that inhibits the activity of the antizyme to ornithine decarboxylase (ODC) was found in rat liver extracts. The factor, ‘antizyme inhibitor’, was heat-labile, non diffusable and of similar molecular size to ODC. The antizyme inhibitor re-activated ODC that had been inactivated by antizyme, apparently by replacing ODC in a ...
K, Fujita, Y, Murakami, S, Hayashi
openaire +2 more sources

