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PYRIMIDINE BIOSYNTHESIS IN NEISSERIA MENINGITIDIS
Author(s) -
JYSSUM SIDSEL
Publication year - 1983
Publication title -
acta pathologica microbiologica scandinavica series b: microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0108-0180
DOI - 10.1111/j.1699-0463.1983.tb00042.x
Subject(s) - pyrimidine metabolism , aspartate carbamoyltransferase , dihydroorotate dehydrogenase , biochemistry , enzyme , ornithine carbamoyltransferase , biology , carbamoyl phosphate synthetase , transferase , chemistry , ornithine , arginine , allosteric regulation , amino acid , purine
Activities of the five enzymes specific for the pyrimidine biosynthetic pathway, aspartate carbamoyltransferase (ACTase), dihydroorotase (DHOase), dihydroorotate dehydrogenase (DHOdehase), orotate phosphoribosyltransferase (OMPppase), and orotidine 5′‐phosphate decarboxylase (OMPdecase) were found in cell‐free extracts of Neisseria meningitidis. Extracts also contained enzyme activities corresponding to the arginine pathway enzyme ornithine carbamoyltransferase (OCTase), and to carbamoylphosphate synthetase (CPSase), the enzyme common to both pathways. N. meningitidis possessed a single glutamine‐dependent CPSase.