Subcellular Localization of the Pathway of de Novo Pyrimidine Nucleotide Biosynthesis in Pea Leaves
Author(s) -
Holly Doremus,
André T. Jagendorf
Publication year - 1985
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.79.3.856
Subject(s) - dihydroorotate dehydrogenase , pyrimidine metabolism , aspartate carbamoyltransferase , chloroplast , biochemistry , nucleotide , biosynthesis , pisum , biology , transferase , enzyme , dehydrogenase , subcellular localization , pyrimidine , adenine phosphoribosyltransferase , plastid , cytoplasm , purine , gene , allosteric regulation
The subcellular distribution of the enzymes of de novo pyrimidine nucleotide biosynthesis was investigated in pea (Pisum sativum L. cv Progress No. 9) leaves. Aspartate carbamoyltransferase, the committed step of the pathway, was found to be strictly confined to the chloroplasts. Dihydro-orotase, orotate phosphoribosyl transferase, and orotidine decarboxylase activities were also found only in the plastids. The remaining enzyme of the pathway, dihydroorotate dehydrogenase, was shown to be mitochondrial.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom