Identification of a glutathione peroxidase homolog in Neisseria meningitidis

被引:6
作者
Aho, EL
Kelly, LP
机构
[1] Department of Biology, Concordia College, Moorhead, MN, 56562
来源
DNA SEQUENCE | 1995年 / 6卷 / 01期
基金
美国国家科学基金会;
关键词
glutathione peroxidase; Neisseria meningitidis; nucleotide sequence; prokaryote;
D O I
10.3109/10425179509074701
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Glutathione peroxidase is an antioxidant enzyme round in a diverse array of eukaryotic species. We have determined the DNA sequence of a glutathione peroxidase homolog in the pathogenic bacterium Neisseria meningitidis. The sequence displays features of a functional gene, but lacks a selenocysteine-encoding in-frame TGA codon characteristic of most mammalian glutathione peroxidase genes. The derived amino acid sequence encoded by the N. meningitidis homolog predicts a 19.9 kDa protein that displays a high level of amino acid identity with other gluathione peroxidase sequences, particularly within four conserved regions of the enzyme.
引用
收藏
页码:55 / 60
页数:6
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