Ray T K, Cronan J E
Proc Natl Acad Sci U S A. 1976 Dec;73(12):4374-8. doi: 10.1073/pnas.73.12.4374.
A soluble enzyme activity which catalyzes the synthesis of acyl-acyl carrier protein from acyl carrier proteins, a long chain fatty acid, and ATP has been demonstrated in E. coli. The reaction requires high concentrations of both Ca++ and Mg++ for activity, and cleaves ATP to AMP and PPi. The fatty acyl product has been identified as acyl-acyl carrier protein by its solubility, thioester linkage, molecular weight, charge, and biological activity. Several criteria indicate the enzyme is distinct from acyl-CoA synthetase. The fatty acid specificity of the enzyme suggests a role of acyl-acyl carrier protein synthetase in the incorporation of fatty acids into phospholipid.
在大肠杆菌中已证实存在一种可溶性酶活性,它能催化由酰基载体蛋白、长链脂肪酸和ATP合成酰基 - 酰基载体蛋白。该反应需要高浓度的Ca++和Mg++才能具有活性,并将ATP裂解为AMP和PPi。通过其溶解性、硫酯键、分子量、电荷和生物活性,已将脂肪酸产物鉴定为酰基 - 酰基载体蛋白。几个标准表明该酶与酰基辅酶A合成酶不同。该酶的脂肪酸特异性表明酰基 - 酰基载体蛋白合成酶在脂肪酸掺入磷脂中的作用。