Haydock S F, Aparicio J F, Molnár I, Schwecke T, Khaw L E, König A, Marsden A F, Galloway I S, Staunton J, Leadlay P F
Cambridge Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge, UK.
FEBS Lett. 1995 Oct 30;374(2):246-8. doi: 10.1016/0014-5793(95)01119-y.
The amino acid sequences of a large number of polyketide synthase domains that catalyse the transacylation of either methylmalonyl-CoA or malonyl-CoA onto acyl carrier protein (ACP) have been compared. Regions were identified in which the acyltransferase sequences diverged according to whether they were specific for malonyl-CoA or methylmalonyl-CoA. These differences are sufficiently clear to allow unambiguous assignment of newly-sequenced acyltransferase domains in modular polyketide synthases. Comparison with the recently-determined structure of the malonyltransferase from Escherichia coli fatty acid synthase showed that the divergent region thus identified lies near the acyltransferase active site, though not close enough to make direct contact with bound substrate.
大量催化丙二酸单酰辅酶A或甲基丙二酸单酰辅酶A转酰基至酰基载体蛋白（ACP）的聚酮合酶结构域的氨基酸序列已被比较。根据丙二酸单酰辅酶A或甲基丙二酸单酰辅酶A的特异性，确定了酰基转移酶序列存在差异的区域。这些差异足够明显，能够明确指定模块化聚酮合酶中新测序的酰基转移酶结构域。与最近确定的大肠杆菌脂肪酸合酶丙二酸单酰转移酶结构比较表明，如此确定的差异区域位于酰基转移酶活性位点附近，尽管距离不足以与结合的底物直接接触。
