Kinetic studies of cytoplasmic and mitochondrial aconitate hydratases from rat liver
- PMID: 755796
Item in Clipboard
Kinetic studies of cytoplasmic and mitochondrial aconitate hydratases from rat liver
Ital J Biochem.
1978 Sep-Oct.
Abstract
The kinetic properties of the cytoplasmic and mitochondrial aconitate hydratases of rat liver have been studied by measuring the formation of the two products from each of the three tricarboxylic acids used as substrate. The kinetic properties of the two enzymes are very similar; the similarity of the Km values for each of the three substrates is particularly remarkable. The results are discussed with particular reference to a possible role of the cytoplasmic aconitate hydratase in the process of gluconeogenesis. With both aconitate hydratases, substrate activation by citrate and D-isocitrate has been observed.
Similar articles
-
Developmental changes of rat liver cytoplasmic and mitochondrial aconitate hydratases.Ital J Biochem. 1978 Sep-Oct;27(5):300-4. Ital J Biochem. 1978. PMID: 755797
-
Parallel partial purification of cytoplasmic and mitochondrial aconitate hydratases from rat liver.Eur J Biochem. 1973 May 2;34(3):455-8. doi: 10.1111/j.1432-1033.1973.tb02779.x. Eur J Biochem. 1973. PMID: 4736701 No abstract available.
-
Inhibition by oxalomalate of rat liver mitochondrial and extramitochondrial aconitate hydratase.Biochem J. 1971 Nov;125(2):557-62. doi: 10.1042/bj1250557. Biochem J. 1971. PMID: 5144758 Free PMC article.
-
Aconitate hydratase of mammals under oxidative stress.Biochemistry (Mosc). 2008 Sep;73(9):957-64. doi: 10.1134/s0006297908090010. Biochemistry (Mosc). 2008. PMID: 18976211 Free PMC article. Review.
-
Citrate: its relation to free magnesium ion concentration and cellular energy.Curr Top Cell Regul. 1992;33:185-207. doi: 10.1016/b978-0-12-152833-1.50016-2. Curr Top Cell Regul. 1992. PMID: 1499333 Review. No abstract available.