In silico identification of a new group of specific bacterial and fungal nitroreductases-like proteins

被引：49

作者：

de Oliveira, Iuri Marques

Pegas Henriques, Joao Antonio

Bonatto, Diego

机构：

[1] UCS, Lab Genet Toxicol 206, Inst Biotechnol, Ctr Ciencias Biol & Saude, Caxias Do Sul, RS, Brazil

[2] Univ Fed Rio Grande do Sul, Ctr Biotechnol, Dept Biofis, Porto Alegre, RS, Brazil

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2007年 / 355卷 / 04期

关键词：

nitroreductases; type; 1; nitroreductase; yeast Frm2p/Hbn1p; bacterial NrlAp; reactive nitrogen oxide species;

D O I：

10.1016/j.bbrc.2007.02.049

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The nitroreductase family comprises a group of FMN- or FAD-dependent and NAD(P)H-dependent enzymes able to metabolize nitrosubstituted compounds. The nitroreductases are found within bacterial and some eukaryotic species. In eukaryotes, there is little information concerning the phylogenetic position and biochemical functions of nitroreductases. The yeast Saccharonlyces cerevisiae has two nitroreductase proteins: Frm2p and Hbn1p. While Frm2p acts in lipid signaling pathway, the function of Hbn1p is unknown. In order to elucidate the function of Frm2p/Hbnlp and the presence of homologous sequences in other prokaryotic and eukaryotic species, we performed an in-depth phylogenetic analysis of these proteins. The results showed that bacterial cells have Frm2p/Hbn1p-like sequences (termed Nr1Ap) forming a distinct clade within the fungal Frm2p/Hbnlp family. Hydrophobic cluster analysis and three-dimensional protein modeling allowed us to compare conserved regions among Nr1Ap and Frm2/Hbn1p proteins. In addition, the possible functions of bacterial Nr1Ap and fungal Frm2p/Hbnlp are discussed. (c) 2007 Elsevier Inc. All rights reserved.

引用

页码：919 / 925

页数：7

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