Seidle Heather, Rangaswamy Vidhya, Couch Robin, Bender Carol L, Parry Ronald J
Department of Chemistry, Rice University, Houston, Texas 77005, USA.
J Bacteriol. 2004 Apr;186(8):2499-503. doi: 10.1128/JB.186.8.2499-2503.2004.
Cfa1 was overproduced in Escherichia coli and Pseudomonas syringae, and the degree of 4'-phosphopantetheinylation was determined. The malonyl-coenzyme A:acyl carrier protein transacylase (FabD) of P. syringae was overproduced and shown to catalyze malonylation of Cfa1, suggesting that FabD plays a role in coronatine biosynthesis. Highly purified Cfa1 did not exhibit self-malonylation activity.
Cfa1在大肠杆菌和丁香假单胞菌中过量表达,并测定了4'-磷酸泛酰巯基乙胺化程度。丁香假单胞菌的丙二酰辅酶A:酰基载体蛋白转酰基酶(FabD)过量表达,并显示可催化Cfa1的丙二酰化,这表明FabD在冠菌素生物合成中发挥作用。高度纯化的Cfa1未表现出自我丙二酰化活性。