从大西洋鳕鱼中分离并鉴定出两个编码两种不同嗜冷弹性蛋白酶的cDNA。

Isolation and characterization of two cDNAs from Atlantic cod encoding two distinct psychrophilic elastases.

作者信息

Gudmundsdóttir E, Spilliaert R, Yang Q, Craik C S, Bjarnason J B, Gudmundsdóttir A

机构信息

Science Institute, University of Iceland, Dunhaga, Reykjavik, Iceland.

出版信息

Comp Biochem Physiol B Biochem Mol Biol. 1996 Apr;113(4):795-801. doi: 10.1016/0305-0491(95)02109-4.

DOI:10.1016/0305-0491(95)02109-4

PMID:8925447

Abstract

The cDNAs encoding two different Atlantic cod elastases have been isolated and sequenced. The predicted amino acid sequences revealed two preproelastases, consisting of a signal peptide, an activation peptide and a mature enzyme of 242 and 239 amino acids. Amino acid sequence identity between the two cod elastases was 60.1% and identity with mammalian elastases ranged from 50-64%. The two cod elastases contain all the major structural features common to serine proteases, such as the catalytic triad His57, Asp102 and Ser195. Both cod elastases have a high content of methionine, consistent with previous findings in psychrophilic fish enzymes.

摘要

编码两种不同大西洋鳕鱼弹性蛋白酶的cDNA已被分离和测序。预测的氨基酸序列显示出两种前弹性蛋白酶原，由信号肽、激活肽和分别含有242和239个氨基酸的成熟酶组成。两种鳕鱼弹性蛋白酶之间的氨基酸序列同一性为60.1%，与哺乳动物弹性蛋白酶的同一性范围为50 - 64%。这两种鳕鱼弹性蛋白酶包含丝氨酸蛋白酶共有的所有主要结构特征，如催化三联体His57、Asp102和Ser195。两种鳕鱼弹性蛋白酶的蛋氨酸含量都很高，这与先前对嗜冷鱼类酶的研究结果一致。