Evolution of phosphagen kinase.: VI.: Isolation, characterization and cDNA-derived amino acid sequence of lombricine kinase from the earthworm Eisenia foetida, and identification of a possible candidate for the guanidine substrate recognition site
Evolution of phosphagen kinase.: VI.: Isolation, characterization and cDNA-derived amino acid sequence of lombricine kinase from the earthworm Eisenia foetida, and identification of a possible candidate for the guanidine substrate recognition site
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DOI：
10.1016/s0167-4838(97)00128-3
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发表时间：
1997-12-05
期刊：
影响因子：
--
通讯作者：
Ellington, WR
中科院分区：
文献类型：
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作者：
Suzuki, T;Kawasaki, Y;Ellington, WR
来自蚯蚓体壁肌肉的 Lombricine 激酶 (LK) 被纯化至均质。该酶被证明是由 40 kDa 亚基组成的二聚体。确定了爱胜蚓 LK 的 370 个残基的 cDNA 衍生氨基酸序列。内部胰蛋白酶肽的化学测序支持了序列的有效性。这是首次报道的龙布里辛激酶氨基酸序列。 Eisenia LK 与肌酸激酶 (CK)、精氨酸激酶 (AK) 和糖氰胺激酶 (GK) 的比对表明显示出显着氨基酸缺失的区域（称为 GS 区域），作为胍底物识别位点的可能候选者。使用所有四种磷酸原激酶的氨基酸序列进行的系统发育分析表明，CK、GK 和 LK 可能是从共同的直接祖先蛋白质进化而来的。 (C) 1997 Elsevier Science B.V.
Lombricine kinase (LK) from the body wall muscle of the earthworm Eisenia foetida was purified to homogeneity. The enzyme was shown to be a dimer consisting of 40 kDa subunits. The cDNA-derived amino acid sequence of 370 residues of Eisenia LK was determined. The validity of the sequence was supported by chemical sequencing of internal tryptic peptides. This is the first reported lombricine kinase amino acid sequence. Alignment of Eisenia LK with those of creatine kinases (CKs), arginine kinases (AKs) and glycocyamine kinase (GK) suggested a region displaying remarkable amino acid deletions (referred to GS region), as a possible candidate for guanidine substrate recognition site. A phylogenetic analysis using amino acid sequences of all four phosphagen kinases indicates that CK, GK and LK probably evolved from a common immediate ancestor protein. (C) 1997 Elsevier Science B.V.