Back to Search
Start Over
Characteristic Variations and Similarities in Biochemical, Molecular, and Functional Properties of Glyoxalases across Prokaryotes and Eukaryotes.
- Source :
-
International journal of molecular sciences [Int J Mol Sci] 2017 Mar 30; Vol. 18 (4). Date of Electronic Publication: 2017 Mar 30. - Publication Year :
- 2017
-
Abstract
- The glyoxalase system is the ubiquitous pathway for the detoxification of methylglyoxal (MG) in the biological systems. It comprises two enzymes, glyoxalase I (GLYI) and glyoxalase II (GLYII), which act sequentially to convert MG into d-lactate, thereby helping living systems get rid of this otherwise cytotoxic byproduct of metabolism. In addition, a glutathione-independent GLYIII enzyme activity also exists in the biological systems that can directly convert MG to d-lactate. Humans and Escherichia coli possess a single copy of GLYI (encoding either the Ni- or Zn-dependent form) and GLYII genes, which through MG detoxification provide protection against various pathological and disease conditions. By contrast, the plant genome possesses multiple GLYI and GLYII genes with a role in abiotic stress tolerance. Plants possess both Ni <superscript>2+</superscript> - and Zn <superscript>2+</superscript> -dependent forms of GLYI, and studies on plant glyoxalases reveal the various unique features of these enzymes distinguishing them from prokaryotic and other eukaryotic glyoxalases. Through this review, we provide an overview of the plant glyoxalase family along with a comparative analysis of glyoxalases across various species, highlighting similarities as well as differences in the biochemical, molecular, and physiological properties of these enzymes. We believe that the evolution of multiple glyoxalases isoforms in plants is an important component of their robust defense strategies.
- Subjects :
- Aldehyde Oxidoreductases chemistry
Aldehyde Oxidoreductases genetics
Animals
Bacterial Proteins chemistry
Bacterial Proteins genetics
Bacterial Proteins metabolism
Evolution, Molecular
Lactoylglutathione Lyase chemistry
Lactoylglutathione Lyase genetics
Plant Proteins chemistry
Plant Proteins genetics
Plants genetics
Thiolester Hydrolases chemistry
Thiolester Hydrolases genetics
Aldehyde Oxidoreductases metabolism
Lactoylglutathione Lyase metabolism
Plant Proteins metabolism
Plants enzymology
Thiolester Hydrolases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1422-0067
- Volume :
- 18
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- International journal of molecular sciences
- Publication Type :
- Academic Journal
- Accession number :
- 28358304
- Full Text :
- https://doi.org/10.3390/ijms18040250