Masumoto Naoko, Lanyon-Hogg Thomas, Rodgers Ursula R, Konitsiotis Antonios D, Magee Anthony I, Tate Edward W
*Department of Chemistry, Imperial College London, South Kensington Campus, London, SW7 2AZ, U.K.
‡Molecular Medicine Section, National Lung & Heart Institute, Sir Alexander Fleming Building, South Kensington Campus, Imperial College London, SW7 2AZ, U.K.
Biochem Soc Trans. 2015 Apr;43(2):246-52. doi: 10.1042/BST20150018.
Since the identification of the membrane-bound O-acyltransferase (MBOATs) protein family in the early 2000s, three distinct members [porcupine (PORCN), hedgehog (Hh) acyltransferase (HHAT) and ghrelin O-acyltransferase (GOAT)] have been shown to acylate specific proteins or peptides. In this review, topology determination, development of assays to measure enzymatic activities and discovery of small molecule inhibitors are compared and discussed for each of these enzymes.
自21世纪初鉴定出膜结合O-酰基转移酶(MBOATs)蛋白家族以来,已发现三个不同的成员[刺猬因子(PORCN)、刺猬酰基转移酶(HHAT)和胃饥饿素O-酰基转移酶(GOAT)]可对特定蛋白质或肽进行酰化。在本综述中,对这些酶中的每一种,都比较并讨论了其拓扑结构的确定、测量酶活性的检测方法的开发以及小分子抑制剂的发现。