The occurrence of nucleotide pyrophosphotransferase (ATP: nucleotide 5'-phosphate pyrophosphotransferase, EC 2.7.4) and the changes in its activity were studied during differentiation in cultures of two Streptomyces griseus strains grown on the surface of a solid medium. One of the strains does not sporulate and produce nucleotide pyro photransferase in submerged culture. Nucleotide pyrophosphotransferase could be detected, though in much differing amounts, in surface cultures of both strains.
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Brain Pathol
November 2018
Facultad de Ciencias y Tecnologías Químicas/Facultad de Medicina de Ciudad Real, Departamento de Química Inorgánica, Orgánica y Bioquímica, Centro Regional de Investigaciones Biomédicas, Universidad de Castilla-La Mancha, Ciudad Real, Spain.
Adenosine, hypoxanthine, xanthine, guanosine and inosine levels were assessed by HPLC, and the activity of related enzymes 5'-nucleotidase (5'-NT), adenosine deaminase (ADA) and purine nucleoside phosphorylase (PNP) measured in frontal (FC), parietal (PC) and temporal (TC) cortices at different stages of disease progression in Alzheimer's disease (AD) and in age-matched controls. Significantly decreased levels of adenosine, guanosine, hypoxanthine and xanthine, and apparently less inosine, are found in FC from the early stages of AD; PC and TC show an opposing pattern, as adenosine, guanosine and inosine are significantly increased at least at determinate stages of AD whereas hypoxanthine and xanthine levels remain unaltered. 5'-NT is reduced in membranes and cytosol in FC mainly at early stages but not in PC, and only at advanced stages in cytosol in TC.
View Article and Find Full Text PDFBiosci Biotechnol Biochem
December 1994
Laboratory of Molecular Gene Technics, Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka, Japan.
Streptomyces ATP nucleotide 3'-pyrophosphokinase is an extracellular enzyme that transfers 5'-beta, gamma-pyrophosphoryl groups of ATP to a variety of nucleotides at the 3'-OH site. The enzyme gene was cloned from partially Sau3AI-digested chromosomal DNA of S. morookaensis in S.
View Article and Find Full Text PDFNucleic Acids Symp Ser
March 1993
Laboratory of Molecular Gene Technics, Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka, Japan.
Streptomyces ATP nucleotide 3'-pyrophosphokinase is an extracellular, ribosome-independent, and stringent factor-mimic ppGpp synthetase with an unusually broad acceptor spectrum. The gene-containing DNA fragments cloned from chromosomal DNA of a producer S. morookaensis into pIJ699 and pUC plasmids were found to express the active enzyme in the transformed S.
View Article and Find Full Text PDFNucleic Acids Symp Ser
September 1991
Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka, Japan.
Streptomyces nucleotide 3'-pyrophosphokinase does not only transfer the 5'-beta, gamma-pyrophosphoryl group of ATP, ATP 3'-pyrophosphate or dATP to a variety of nucleotides at the 3'-OH site, but also adds 2',3'-cyclic terminal monophosphate to some suitable nucleotides with the use of diadenosine 5',5'-polyphosphates (n = 3-5). Examples are pA greater than p, ppA greater than p, pG greater than p, CpG greater than p, etc.
View Article and Find Full Text PDFJ Basic Microbiol
May 1990
Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka, Japan.
The synthesis of GTP- and ATP-3'-pyrophosphate by Streptomyces morookaensis nucleotide 3'-pyrophosphokinase was little affected by the presence of a ribosome-deacylated tRNA-poly A, G, U mixture in vitro. The Streptomyces pyrophosphokinases thus do not appear, unlike bacterial stringent factors, to play a significant role in the cellular stringent control.
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