Barley acyl carrier protein: Its amino acid sequence and assay using purified malonyl-CoA:ACP transacylase
Barley acyl carrier protein: Its amino acid sequence and assay using purified malonyl-CoA:ACP transacylase
复制标题
大麦酰基载体蛋白：其氨基酸序列和使用纯化的丙二酰辅酶A:ACP转酰基酶的测定
DOI：
--
复制
发表时间：
1983
期刊：
影响因子：
--
通讯作者：
I. Svendsen
中科院分区：
文献类型：
--
作者：
P. Høj;I. Svendsen
丙二酰辅酶A：来自大麦（Hordeum vulgare L.）已被纯化至同质并用于酰基载体蛋白（ACP）的测定。转酰酶是一种酸性单体蛋白质，分子量为34，500，与类似的E。已将来自大麦的热和酸稳定的酰基载体蛋白纯化至均一，并测定其化学组成。ACP由以下72个氨基酸的连续延伸组成H2 N-A-A-M-G-E-A-Q-A-K-K-E-T-V-D-K-V-（C？）- M-I-V-K-K-Q-L-A-V-P-D-G-T-P-V-T-A-E-S-K-F-S-E-L-G-A-D-S-L-D-T-V-E-I-V-M-G-L-E-E-E-F-N-I-T-V-D-E-T-S-A-Q-D-I-A72. A87-COOH。对这种植物ACP和细菌ACP的一级结构进行比较，发现在含有4 '-磷酸泛酰巯基乙胺附着位点的分子中部区域有两个相同的序列（加下划线），而在该区域之外存在差异。9个额外的残基（斜体）存在于大麦蛋白的N-末端，从而解释了其较大的尺寸。将大麦叶绿体脂肪酸合成酶与大麦或E. coliACP，但后者在脂肪酸合成方面的活性是前者的两倍。ACP的N-末端部分的可能意义进行了讨论，在有关植物和细菌ACP的生化活性的差异报道。
Malonyl-CoA:ACP transacylase from barley (Hordeum vulgare L.) has been purified to homogeneity and used in an assay for acyl carrier protein (ACP). The transacylase is an acidic, monomeric protein with a molecular weight of 34,500 very similar to the analogous E. coli enzyme.A heat and acid stable acyl carrier protein from barley has been purified to homogeneity and its chemical composition determined. The ACP consists of a continuous stretch of the following 72 amino acids H2N-A-A-M-G-E-A-Q-A-K-K-E-T-V-D-K-V-(C?)-M-I-V-K-K-Q-L-A-V-P-D-G-T-P-V-T-A-E-S-K-F-S-E-L-G-A-D-S-L-D-T-V-E-I-V-M-G-L-E-E-E-F-N-I-T-V-D-E-T-S-A-Q-D-I-A72...A87-COOH. A comparison of the primary structure of this plant ACP and bacterial ACP reveals two identical sequences (underlined) in the midregion of the molecule containing the 4′-phosphopantetheine attachment site, while differences occur outside this region. Nine extra residues (italicized) are present at the N-terminal end of the barley protein thereby accounting for its larger size. Identical products are obtained when barley chloroplast fatty acid synthetase is incubated with either barley or E. coli ACP, but the latter is twice as active as the former in fatty acid synthesis. The possible significance of the N-terminal part of the ACP is discussed in relation to the reported differences in biochemical activities of plant and bacterial ACPs.