ATP+Mg2+对大鼠肝微粒体中酰基辅酶A：胆固醇酰基转移酶的失活作用。
Inactivation of acyl-CoA:cholesterol acyltransferase by ATP+Mg2+ in rat liver microsomes.
作者信息
Kwok C T, Smith J L, Pillay S P, Hardie I R
出版信息
Biochem Int. 1984 Feb;8(2):271-82.
The molecular modulation of acyl-CoA:cholesterol acyltransferase (EC 2.3.2.26) was studied in the microsomes of rat liver. Acyl-CoA: cholesterol acyltransferase was specifically inactivated by ATP and ADP, requiring Mg2+ as a cofactor. The inactivation was not due to substrate diminution nor to inhibition by the activity of acyl-CoA hydrolase, which was not affected by Mg2+ or ATP+Mg2+. Enhancement of inactivation of acyl-CoA: cholesterol acyltransferase by ATP+Mg2+, NaF and a heat-labile cytosolic factor (or factors) is consistent with a protein-kinase catalyzed phosphorylation being involved in the short term regulation of this enzyme.
在大鼠肝脏微粒体中研究了酰基辅酶A：胆固醇酰基转移酶（EC 2.3.2.26）的分子调节。酰基辅酶A：胆固醇酰基转移酶被ATP和ADP特异性失活，需要Mg2+作为辅因子。失活不是由于底物减少，也不是由于酰基辅酶A水解酶活性的抑制，该水解酶不受Mg2+或ATP + Mg2+的影响。ATP + Mg2+、NaF和一种热不稳定的胞质因子（或多种因子）增强酰基辅酶A：胆固醇酰基转移酶的失活，这与蛋白激酶催化的磷酸化参与该酶的短期调节是一致的。
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