磷酸原激酶的进化（III）。日本对虾精氨酸激酶的氨基酸序列。

Evolution of phosphagen kinase (III). Amino acid sequence of arginine kinase from the shrimp Penaeus japonicus.

作者信息

Furukohri T, Okamoto S, Suzuki T

机构信息

Department of Biology, Faculty of Science, Kochi University, Japan.

出版信息

Zoolog Sci. 1994 Apr;11(2):229-34.

PMID:7765044

Abstract

The amino acid sequence of arginine kinase (AK) from the shrimp Penaeus japonicus has been determined chemically. It consists of 355 amino acid residues, and has a calculated molecular mass of 40,018 Da. The amino acid sequence of Penaeus AK showed 91% and 51% identity, respectively, with those of AKs from the lobster Homarus vulgaris and the abalone Nordotis madaka. It also showed significant homology (39-43%) with vertebrate or invertebrate creatine kinases and annelid glycocyamine kinase, suggesting that these enzymes evolved from a common origin.

摘要

日本对虾精氨酸激酶（AK）的氨基酸序列已通过化学方法测定。它由355个氨基酸残基组成，计算分子量为40,018道尔顿。日本对虾AK的氨基酸序列与龙虾（美洲螯龙虾）和鲍鱼（盘鲍）的AK氨基酸序列分别具有91%和51%的同一性。它还与脊椎动物或无脊椎动物的肌酸激酶以及环节动物胍基乙胺激酶具有显著的同源性（39 - 43%），这表明这些酶起源于共同的祖先。