Reuner C, Hable M, Wilmanns M, Kiefer E, Schiltz E, Schulz G E
Institut für Organische Chemie und Biochemie der Universität, Freiburg, Federal Republic of Germany.
Protein Seq Data Anal. 1988;1(5):335-43.
The amino acid sequence of cytosolic adenylate kinase from carp muscle has been determined. For the analysis of the blocked amino terminus an N-acylaminoacyl peptidase has been isolated and applied successfully. The resulting sequence is homologous to those of other adenylate kinases. It has 76% and 74% identical amino acids when compared with the enzymes from chicken and pig, respectively. The carp enzyme forms X-ray-grade crystals, the structure of which has been solved at 0.58-nm resolution. The observed chain fold is very similar to the known fold of the porcine enzyme in crystal form-A, whereas the molecular packing arrangements are quite different. This finding confirms that the observed porcine enzyme structure is intrinsically stable and has not been enforced during the crystallization process. The sequence of cytosolic adenylate kinase from carp muscle is: (table; see text)
鲤鱼肌肉胞质腺苷酸激酶的氨基酸序列已被确定。为了分析封闭的氨基末端，一种N-酰基氨基酸酰基肽酶已被分离并成功应用。所得序列与其他腺苷酸激酶的序列同源。与鸡和猪的酶相比，它分别有76%和74%的相同氨基酸。鲤鱼酶形成了X射线级晶体，其结构已在0.58纳米分辨率下解析。观察到的链折叠与晶体形式A中猪酶的已知折叠非常相似，而分子堆积排列则大不相同。这一发现证实，观察到的猪酶结构本质上是稳定的，在结晶过程中并未受到强制作用。鲤鱼肌肉胞质腺苷酸激酶的序列如下：（表格；见正文）
