Suzuki T, Kawasaki Y, Furukohri T, Ellington W R
Department of Biology, Faculty of Science, Kochi University, Japan.
Biochim Biophys Acta. 1997 Dec 5;1343(2):152-9. doi: 10.1016/s0167-4838(97)00128-3.
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.
从蚯蚓赤子爱胜蚓体壁肌肉中纯化出了地龙激酶（LK），使其达到了均一性。该酶被证明是由40 kDa亚基组成的二聚体。测定了赤子爱胜蚓370个残基的cDNA推导氨基酸序列。内部胰蛋白酶肽段的化学测序支持了该序列的有效性。这是首次报道的地龙激酶氨基酸序列。将赤子爱胜蚓LK与肌酸激酶（CKs）、精氨酸激酶（AKs）和胍基乙胺激酶（GK）的序列进行比对，发现了一个显示出显著氨基酸缺失的区域（称为GS区域），该区域可能是胍底物识别位点的候选区域。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可能从一个共同的直接祖先蛋白进化而来。
