Arthur Christopher J, Szafranska Anna E, Long Jed, Mills Jane, Cox Russell J, Findlow Stuart C, Simpson Thomas J, Crump Matthew P, Crosby John
School of Chemistry, University of Bristol, Cantock's Close, Bristol BS8 1TS, United Kingdom.
Chem Biol. 2006 Jun;13(6):587-96. doi: 10.1016/j.chembiol.2006.03.010.
Acyl carrier proteins (ACPs) play a fundamental role in directing intermediates among the enzyme active sites of fatty acid and polyketide synthases (PKSs). In this paper, we demonstrate that the Streptomyces coelicolor (S. coelicolor) actinorhodin (act) PKS ACP can catalyze transfer of malonate to type II S. coelicolor fatty acid synthase (FAS) and other PKS ACPs in vitro. The reciprocal transfer from S. coelicolor FAS ACP to a PKS ACP was not observed. Several mutations in both act ACP and S. coelicolor FAS ACP could be classified by their participation in either donation or acceptance of this malonyl group. These mutations indicated that self-malonylation and malonyl transfer could be completely decoupled, implying that they were separate processes and that a FAS ACP could be converted from a non-malonyl-transferring protein to one with malonyl transferase activity.
酰基载体蛋白（ACPs）在引导脂肪酸和聚酮合酶（PKSs）的酶活性位点之间的中间体方面发挥着重要作用。在本文中，我们证明了天蓝色链霉菌（S. coelicolor）放线紫红素（act）聚酮合酶ACPs能够在体外催化丙二酸酯转移至II型天蓝色链霉菌脂肪酸合酶（FAS）和其他聚酮合酶ACPs。未观察到从天蓝色链霉菌FAS ACP到聚酮合酶ACPs的反向转移。act ACP和天蓝色链霉菌FAS ACP中的几个突变可根据它们参与该丙二酰基的捐赠或接受情况进行分类。这些突变表明自我丙二酰化和丙二酰基转移可以完全解偶联，这意味着它们是独立的过程，并且FAS ACP可以从非丙二酰基转移蛋白转变为具有丙二酰基转移酶活性的蛋白。
