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Int. J. Mol. Sci. 2017, 18(4), 250; doi:10.3390/ijms18040250

Characteristic Variations and Similarities in Biochemical, Molecular, and Functional Properties of Glyoxalases across Prokaryotes and Eukaryotes

1
Stress Physiology and Molecular Biology Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India
2
Plant Stress Biology Group, International Centre for Genetic Engineering and Biotechnology, New Delhi 110067, India
3
Department of Plant Molecular Biology, University of Delhi South campus, New Delhi 110021, India
*
Author to whom correspondence should be addressed.
Academic Editor: Casper G. Schalkwijk
Received: 14 December 2016 / Revised: 14 January 2017 / Accepted: 18 January 2017 / Published: 30 March 2017
(This article belongs to the Special Issue Glyoxalase System)
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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 Ni2+- and Zn2+-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. View Full-Text
Keywords: glyoxalase pathway; glyoxalase III; methylglyoxal; multigene family; plants; abiotic stress tolerance; prokaryotes glyoxalase pathway; glyoxalase III; methylglyoxal; multigene family; plants; abiotic stress tolerance; prokaryotes
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Kaur, C.; Sharma, S.; Hasan, M.R.; Pareek, A.; Singla-Pareek, S.L.; Sopory, S.K. Characteristic Variations and Similarities in Biochemical, Molecular, and Functional Properties of Glyoxalases across Prokaryotes and Eukaryotes. Int. J. Mol. Sci. 2017, 18, 250.

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