@article{mbs:/content/journal/micro/10.1099/00221287-16-2-426, author = "Smith, Evelyn E. B. and Mills, G. T. and Harper, Elizabeth M.", title = "A Comparison of the Uridine Pyrophosphoglycosyl Metabolism of Capsulated and Non-capsulated Pneumococci", journal= "Microbiology", year = "1957", volume = "16", number = "2", pages = "426-437", doi = "https://doi.org/10.1099/00221287-16-2-426", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-16-2-426", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "SUMMARY: A study has been made of the uridine pyrophosphoglycosyl compounds present in a non-capsulated pneumococcus (Streptococcus pneumoniae, strain R19, derived from a type II organism) and a capsulated pneumococcus (type III; Streptococcus pneumoniae, strain A66), and also of certain enzymes involved in the metabolism of these compounds. It has been found that both the pneumococcal strains contained considerable amounts of uridine pyrophosphoglucuronic acid (UPPGA) and uridine pyrophosphoacetylglucosamine (UPPAG), with lesser amounts of uridine pyrophosphoglucose (UPPG), uridine-5′-monophosphate (UMP), uridine pyrophosphate (UPP) and uridine triphosphate (UTP). The patterns shown by these two strains with respect to uridine nucleotide content were very similar. Cell-free extracts of strain R19, derived from a type II organism, were obtained; these extracts contained the following enzymes: glucose-6-phosphate dehydrogenase, uridyl transferase, inorganic pyrophosphatase, nucleoside diphosphokinase, hexo- kinase and phosphoglucomutase. Examination of the strain A 66 capsulated (type III) organism showed the presence of uridyl transferase, nucleoside diphosphokinase and inorganic pyrophosphatase.", }