DIVERGENT SEQUENCE MOTIFS CORRELATED WITH THE SUBSTRATE-SPECIFICITY OF (METHYL)MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE DOMAINS IN MODULAR POLYKETIDE SYNTHESES
DIVERGENT SEQUENCE MOTIFS CORRELATED WITH THE SUBSTRATE-SPECIFICITY OF (METHYL)MALONYL-COA-ACYL CARRIER PROTEIN TRANSACYLASE DOMAINS IN MODULAR POLYKETIDE SYNTHESES
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DOI：
10.1016/0014-5793(95)01119-y
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发表时间：
1995-10-30
期刊：
影响因子：
3.5
通讯作者：
LEADLAY, PF
中科院分区：
文献类型：
--
作者：
HAYDOCK, SF;APARICIO, JF;LEADLAY, PF
已经比较了催化甲基丙二酰-CoA或丙二酰-CoA转酰到酰基载体蛋白（ACP）上的大量聚酮合酶结构域的氨基酸序列。鉴定了其中酰基转移酶序列根据它们是否特异于丙二酰-CoA或甲基丙二酰-CoA而不同的区域，这些差异是足够清楚的，允许明确分配模块化聚酮酶中的新测序的酰基转移酶结构域。与最近确定的结构的丙二酰转移酶从大肠杆菌脂肪酸合酶的比较表明，分歧的区域，从而确定位于附近的酰基转移酶活性位点，但不够接近，使直接接触结合底物。
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.