猪心脏柠檬酸合酶的一级结构。
Primary structure of porcine heart citrate synthase.
作者信息
Bloxham D P, Parmelee D C, Kumar S, Wade R D, Ericsson L H, Neurath H, Walsh K A, Titani K
出版信息
Proc Natl Acad Sci U S A. 1981 Sep;78(9):5381-5. doi: 10.1073/pnas.78.9.5381.
Abstract
The sequence of 437 amino acid residues of porcine heart citrate synthase [citrate oxaloacetate-lyase (pro-3S-CH2COO leads to acetyl-CoA), EC 4. 1. 3. 7] has been determined by the alignment of fragments generated by cleavage with cyanogen bromide and with trypsin. Isolation of the peptides was facilitated by recent developments in the high-performance liquid chromatography of peptide mixtures. The alignment of these peptides was consistent with that previously deduced from fragments derived by restricted cleavage of citrate synthase by limited proteolysis and cleavage of aspartyl-prolyl bonds and asparaginyl-glycyl bonds. The enzyme contains a modified amino acid, trimethyllysine, at residue 368, showing that the enzyme is subjected to post-translational modification.
摘要
通过对溴化氰和胰蛋白酶切割产生的片段进行比对，已确定猪心柠檬酸合酶[柠檬酸草酰乙酸裂解酶（pro-3S-CH2COO生成乙酰辅酶A），EC 4.1.3.7]的437个氨基酸残基序列。肽混合物高效液相色谱技术的最新进展有助于肽的分离。这些肽的比对结果与先前从柠檬酸合酶经有限蛋白酶解以及天冬氨酰-脯氨酰键和天冬氨酰-甘氨酰键的限制性切割所产生的片段推导得出的结果一致。该酶在第368位残基处含有一个修饰氨基酸——三甲基赖氨酸，这表明该酶经历了翻译后修饰。
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