formycin has been researched along with pyrazofurin* in 3 studies
3 other study(ies) available for formycin and pyrazofurin
Article | Year |
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Identification of the C-Glycoside Synthases during Biosynthesis of the Pyrazole-C-Nucleosides Formycin and Pyrazofurin.
C-Nucleosides are characterized by a C-C rather than a C-N linkage between the heterocyclic base and the ribofuranose ring. While the biosynthesis of pseudouridine-C-nucleosides has been studied, less is known about the pyrazole-C-nucleosides such as the formycins and pyrazofurin. Herein, genome screening of Streptomyces candidus NRRL 3601 led to the discovery of the pyrazofurin biosynthetic gene cluster pyf. In vitro characterization of gene product PyfQ demonstrated that it is able to catalyze formation of the C-glycoside carboxyhydroxypyrazole ribonucleotide (CHPR) from 4-hydroxy-1H-pyrazole-3,5-dicarboxylic acid and phosphoribosyl pyrophosphate (PRPP). Similarly, ForT, the PyfQ homologue in the formycin pathway, can catalyze the coupling of 4-amino-1H-pyrazole-3,5-dicarboxylic acid and PRPP to form carboxyaminopyrazole ribonucleotide. Finally, PyfP and PyfT are shown to catalyze amidation of CHPR to pyrazofurin 5'-phosphate thereby establishing the latter stages of both pyrazofurin and formycin biosynthesis. Topics: Amides; Bacterial Proteins; Formycins; Glycosides; Multigene Family; Nucleosides; Pyrazoles; Ribonucleosides; Ribose; Streptomyces | 2019 |
Immunological studies with different classes of mutants affected at the adenosine kinase locus in CHO cells.
Adenosine kinase (AK) from CHO cells has been purified to homogeneity and specific antibodies to it have been raised in rabbits. Using this antibody, the presence of a specific cross-reacting protein (CRP) in cell extracts of different classes of mutants resistant to purine nucleoside analogs which are affected in AK has been investigated by the immunoblotting technique. Results of our studies show that 31 of the 32 independently selected class A AK- mutants (obtained at high frequency in presence of adenosine analogs toyocamycin, tubercidin, 6-methylmercaptopurine riboside, or pyrazofurin and containing no measurable activity of AK in cell extracts) contained similar amounts of a specific CRP as seen in the parental AK+ cells. The CRP in the parental and different mutant cell lines has the same relative molecular mass as purified AK. Similar results were obtained with two mutants each of the class B and C type (selected in presence of C-nucleosides formycin A and formycin B), which are also affected in AK but show novel properties. The presence of equivalent amounts of the CRP in the vast majority of the class A mutants strongly indicates that the high frequency of those mutants in CHO cells is not a result of an epigenetic or deletion type of event, but that such mutants may contain missense types of mutations at a presumed "mutational hot spot" within the structural gene for adenosine kinase. Topics: Adenosine Kinase; Amides; Animals; Antibody Specificity; Cell Line; Cricetinae; Cricetulus; Cross Reactions; Drug Resistance; Female; Formycins; Immunosorbent Techniques; Methylthioinosine; Mutation; Ovary; Phosphotransferases; Pyrazoles; Ribonucleosides; Ribose; Toyocamycin; Tubercidin | 1986 |
Involvement of adenosine kinase in the phosphorylation of formycin B in CHO cells.
In Chinese hamster ovary cells, [3H]formycin B is metabolized into formycin B-5'-monophosphate, formycin A-5'-monophosphate and higher phosphorylated derivatives of formycin A which are incorporated into RNA. Mutants of CHO cells independently selected for resistance to various adenosine analogs viz. toyocamycin, tubercidin, 6-methylmercaptopurine riboside, which contain no detectable activity of adenosine kinase (AK) in cell extracts, all exhibited between 2- to 3-fold increased resistance to formycin B. Formycin B-resistant mutants of CHO cells are also affected in AK, as indicated by the absence of AK activity in cell extracts. Both types of AK- mutants showed reduced uptake and phosphorylation of [3H]formycin B in comparison to the parental (AK+) cells. In addition, toxicity of formycin B towards CHO cells was reduced in presence of adenosine in a concentration dependent manner. These observations strongly indicate that in CHO cells, formycin B is phosphorylated via AK and that like other nucleoside analogs its phosphorylation may be essential for the drugs cellular toxicity. Topics: Adenosine; Adenosine Kinase; Amides; Animals; Antibiotics, Antineoplastic; Cell Line; Cricetinae; Drug Resistance; Female; Formycins; Methylthioinosine; Mutation; Ovary; Phosphorylation; Phosphotransferases; Pyrazoles; Ribonucleosides; Ribose; Toyocamycin; Tubercidin | 1985 |