The aspartate transcarbamoylase-dihydroorotase complex in Deinococcus radiophilus has an active dihydroorotase

Arch Microbiol. 2006 Mar;185(1):78-81. doi: 10.1007/s00203-005-0075-3. Epub 2006 Jan 5.

Abstract

Aspartate transcarbamoylase (ATCase) and dihydroorotase (DHOase) catalyse the first two steps unique to pyrimidine synthesis. In many bacteria they form non-covalently bonded complexes. There are two types of DHOase, type I and type II which share a common ancestry. Type I is the more ancient form and is present in the complexes. In recently evolved bacteria the DHOase is defective and its function has been replaced by a type II DHOase which is separate from the complex. Deinococcus radiophilus diverges early on the phylogenetic tree and so might be expected to have an active type I DHOase. Purification of the 500 kDa ATCase-DHOase complex, by conventional techniques, showed it to possess an active DHOase.

MeSH terms

  • Aspartate Carbamoyltransferase / chemistry
  • Aspartate Carbamoyltransferase / metabolism*
  • Chromatography / methods
  • Deinococcus / enzymology*
  • Dihydroorotase / chemistry
  • Dihydroorotase / metabolism*
  • Multienzyme Complexes / chemistry
  • Multienzyme Complexes / metabolism*
  • Pyrimidines / biosynthesis
  • Soil Microbiology

Substances

  • Multienzyme Complexes
  • Pyrimidines
  • Aspartate Carbamoyltransferase
  • Dihydroorotase
  • pyrimidine