pubmed.ncbi.nlm.nih.gov

Localization of carbamoylphosphate synthetase and aspartate carbamoyltransferase in chloroplasts - PubMed

Localization of carbamoylphosphate synthetase and aspartate carbamoyltransferase in chloroplasts

H Shibata et al. Plant Physiol. 1986 Jan.

Abstract

The localization of carbamoylphosphate synthetase (CPSase) and aspartate carbamoyltransferase (ACTase), the first two enzymes of the pyrimidine biosynthetic pathway, in chloroplasts was investigated. In dark-grown radish (Raphanus sativus) seedlings, light induced a prominent increase in CPSase activity, but had little effect on ACTase activity. Both enzymes were found in chloroplasts isolated from radish cotyledons and leaves of spinach (Spinacia oleracea), soybean (Glycine max), and corn (Zea mays). The higher activity of ACTase relative to CPSase is discussed in relation to the instability of carbamoylphosphate, the product of the CPSase, and to the control of pyrimidine synthesis. Based on these results, the function of CPSase and ACTase in chloroplasts is discussed.

PubMed Disclaimer

Similar articles

Cited by

References

    1. J Bacteriol. 1975 Aug;123(2):604-15 - PubMed
    1. Biochem Biophys Res Commun. 1978 Aug 14;83(3):1084-92 - PubMed
    1. Biochemistry. 1964 Sep;3:1238-47 - PubMed
    1. Biochim Biophys Acta. 1982 Sep 17;718(1):1-10 - PubMed
    1. Plant Physiol. 1976 Jan;57(1):23-8 - PubMed

LinkOut - more resources