Isolation and sequencing of a gene coding for glyoxalase I activity from Salmonella typhimurium and comparison with other glyoxalase I sequences

被引：28

作者：

Clugston, SL ^{[1
]}

Daub, E ^{[1
]}

Kinach, R ^{[1
]}

Miedema, D ^{[1
]}

Barnard, JFJ ^{[1
]}

Honek, JF ^{[1
]}

机构：

[1] UNIV WATERLOO,DEPT CHEM,WATERLOO,ON N2L 3G1,CANADA

来源：

GENE | 1997年 / 186卷 / 01期

基金：

加拿大自然科学与工程研究理事会;

关键词：

S-D-lactoylglutathione methylglyoxal lyase; Zn2+ ligands; isomerase;

D O I：

10.1016/S0378-1119(96)00691-9

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

The glyoxalase I gene (gloA) from Salmonella typhimurium has been isolated in Escherichia coli on a multi-copy pBR322-derived plasmid, selecting for resistance to 3 mM methylglyoxal on Luria-Bertani agar. The region of the plasmid which confers the methylglyoxal resistance in E. coli was sequenced. The deduced protein sequence was compared to the known sequences of the Home sapiens and Pseudomonas putida glyoxalase I (GlxI) enzymes, and regions of strong homology were used to probe the National Center for Biotechnology Information protein database. This search identified several previously known glyoxalase I sequences and other open reading frames with unassigned function. The clustal alignments of the sequences are presented, indicating possible Zn2+ ligands and active site regions. In addition, the S. typhimurium sequence aligns with both the N-terminal half and the C-terminal half of the proposed GlxI sequences from Saccharomyces cerevisiae and Schizosaccharomyces pombe, suggesting that the structures of the yeast enzymes are those of fused dimers.

引用

页码：103 / 111

页数：9

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