High impact information on Acot7

• Comparison of physical and catalytical characteristics of the enzymes studied here and previously purified acyl-CoA thioesterases suggest that MTE-I and MTE-II are novel enzymes [1].
• The second enzyme was partially purified and characterized as a long chain acyl-CoA thioesterase (MTE-II) [1].
• In the liver cytosol of rats treated with di(2-ethylhexyl)phthalate, about 90% of palmitoyl-CoA hydrolase activity was titrated with anti-ACH1 and anti-ACH2 antibodies [2].
• A marked difference in their catalytic properties was found in the maximal velocity; for palmitoyl-CoA, 553 and 4.23 mumol/min/mg with Km values of 5.9 and 5.4 microM for ACH1 and ACH2, respectively [2].
• Immunoblot analysis suggested the presence of the enzymes also in extrahepatic tissues, especially in the brain and testis (ACH1), and in the heart and kidney (ACH2) [2].

Biological context of Acot7

• The mechanism of cytogenetic genotoxicity (clastogenicity, induction, cell cycle delay) of 10(-3) M glutathione in V79-E cells, as described by Thust and Bach (1985), was studied in detail by using different treatment conditions [3].

Associations of Acot7 with chemical compounds

• Two long-chain acyl-CoA hydrolases, referred to as ACH1 and ACH2, were purified from the liver cytosol of rats fed a diet containing di(2-ethylhexyl)phthalate, a peroxisome proliferator [2].

Analytical, diagnostic and therapeutic context of Acot7

• Molecular cloning and expression of cDNA encoding rat brain cytosolic acyl-coenzyme A thioester hydrolase [4].
• The molecular mass of ACH1 was estimated to be 73 kDa by gel filtration, and that of the subunits, 36 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis [2].
• A quantitative evaluation of the data was carried out by use of the barrier-limited, space-distributed variable transit time model (C.A. Goresky, G.G. Bach, and B. E. Nadeau, J. Clin. Invest. 52:991-1009, 1973) [5].

References