山羊乳腺脂肪酸合成酶酰基转移酶结构域中活性位点丝氨酸残基周围的氨基酸序列。
Amino acid sequence around the active-site serine residue in the acyltransferase domain of goat mammary fatty acid synthetase.
作者信息
Mikkelsen J, Højrup P, Rasmussen M M, Roepstorff P, Knudsen J
出版信息
Biochem J. 1985 Apr 1;227(1):21-7. doi: 10.1042/bj2270021.
Abstract
Goat mammary fatty acid synthetase was labelled in the acyltransferase domain by formation of O-ester intermediates by incubation with [1-14C]acetyl-CoA and [2-14C]malonyl-CoA. Tryptic-digest and CNBr-cleavage peptides were isolated and purified by high-performance reverse-phase and ion-exchange liquid chromatography. The sequences of the malonyl- and acetyl-labelled peptides were shown to be identical. The results confirm the hypothesis that both acetyl and malonyl groups are transferred to the mammalian fatty acid synthetase complex by the same transferase. The sequence is compared with those of other fatty acid synthetase transferases.
摘要
通过与[1-¹⁴C]乙酰辅酶A和[2-¹⁴C]丙二酰辅酶A孵育形成O-酯中间体，对山羊乳腺脂肪酸合成酶的酰基转移酶结构域进行标记。通过高效反相和离子交换液相色谱法分离并纯化胰蛋白酶消化肽和溴化氰裂解肽。结果表明，丙二酰标记肽和乙酰标记肽的序列相同。这些结果证实了如下假设：乙酰基和丙二酰基均由同一种转移酶转移至哺乳动物脂肪酸合成酶复合体。将该序列与其他脂肪酸合成酶转移酶的序列进行了比较。
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本文引用的文献
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Analysis of amino acid phenylthiohydantoins by high-performance liquid chromatography using gradient elution with ethanol.使用乙醇梯度洗脱的高效液相色谱法分析氨基酸苯硫代乙内酰脲。
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