scholarly journals Presence of unique glyoxalase III proteins in plants indicates the existence of shorter route for methylglyoxal detoxification

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Ajit Ghosh ◽  
Hemant R Kushwaha ◽  
Mohammad R Hasan ◽  
Ashwani Pareek ◽  
Sudhir K Sopory ◽  
...  
Keyword(s):  
Glyoxalase Iii

Functional characterization and expression profiling of glyoxalase III genes in date palm grown under abiotic stresses

2020 ◽  
Author(s):  
Gerry A. Jana ◽  
Pannaga Krishnamurthy ◽  
Prakash P. Kumar ◽  
Mahmoud W. Yaish
Keyword(s):  
Expression Profiling ◽  
Abiotic Stresses ◽  
Date Palm ◽  
Functional Characterization ◽  
Glyoxalase Iii

scholarly journals Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into d-lactate without reduced glutathione

1995 ◽  
Vol 305 (3) ◽  
pp. 999-1003 ◽  
Author(s):  
K Misra ◽  
A B Banerjee ◽  
S Ray ◽  
M Ray
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Carbonyl Compounds ◽  
Reduced Glutathione ◽  
Thiol Group ◽  
Glyoxalase I ◽  
Ph Optimum ◽  
Native Form ◽  
Wide Range ◽  
Glyoxalase Iii

A single novel enzyme, glyoxalase III, which catalyses the conversion of methylglyoxal into D-lactate without involvement of GSH, has been detected in and purified from Escherichia coli. Of several carbonyl compounds tested, only the alpha-ketoaldehydes methylglyoxal and phenylglyoxal were found to be substrates for this enzyme. Glyoxalase III is active over a wide range of pH with no sharp pH optimum. In its native form it has an M(r) of 82000 +/- 2000, and it is composed of two subunits of equal M(r). Glutathione analogues, which are inhibitors of glyoxalase I, do not inhibit glyoxalase III. Glyoxalase III is found to be sensitive to thiol-blocking reagents. The p-hydroxymercuribenzoate-inactivated enzyme could be almost completely re-activated by dithiothreitol and other thiol-group-containing compounds, indicating the possible involvement of thiol group(s) at or near the active site of the enzyme.

scholarly journals Structural and functional studies of SAV0551 from Staphylococcus aureus as a chaperone and glyoxalase III

2017 ◽  
Vol 37 (6) ◽  
Author(s):  
Hyo Jung Kim ◽  
Ki-Young Lee ◽  
Ae-Ran Kwon ◽  
Bong-Jin Lee
Keyword(s):  
Staphylococcus Aureus ◽  
Reaction Mechanism ◽  
Quaternary Structure ◽  
Hypothetical Protein ◽  
Catalytic Triad ◽  
Common Theme ◽  
Functional Studies ◽  
The Common ◽  
Cellular Stresses ◽  
Glyoxalase Iii

The DJ-1/ThiJ/PfpI superfamily of proteins is highly conserved across all biological kingdoms showing divergent multifunctions, such as chaperone, catalase, protease, and kinase. The common theme of these functions is responding to and managing various cellular stresses. DJ-1/ThiJ/PfpI superfamily members are classified into three subfamilies according to their quaternary structure (DJ-1-, YhbO-, and Hsp-types). The Hsp-type subfamily includes Hsp31, a chaperone and glyoxalase III. SAV0551, an Hsp-type subfamily member from Staphylococcus aureus, is a hypothetical protein that is predicted as Hsp31. Thus, to reveal the function and reaction mechanism of SAV0551, the crystal structure of SAV0551 was determined. The overall folds in SAV0551 are similar to other members of the Hsp-type subfamily. We have shown that SAV0551 functions as a chaperone and that the surface structure is crucial for holding unfolded substrates. As many DJ-1/ThiJ/PfpI superfamily proteins have been characterized as glyoxalase III, our study also demonstrates SAV0551 as a glyoxalase III that is independent of any cofactors. The reaction mechanism was evaluated via a glyoxylate-bound structure that mimics the hemithioacetal reaction intermediate. We have confirmed that the components required for reaction are present in the structure, including a catalytic triad for a catalytic action, His78 as a base, and a water molecule for hydrolysis. Our functional studies based on the crystal structures of native and glyoxylate-bound SAV0551 will provide a better understanding of the reaction mechanism of a chaperone and glyoxalase III.

scholarly journals Hsp31 of Escherichia coli K-12 is glyoxalase III

2011 ◽  
Vol 81 (4) ◽  
pp. 926-936 ◽  
Author(s):  
Krishna P. Subedi ◽  
Dongwook Choi ◽  
Insook Kim ◽  
Bumchan Min ◽  
Chankyu Park
Keyword(s):  
Escherichia Coli ◽  
K 12 ◽  
Glyoxalase Iii

scholarly journals Oxidative stress triggers aggregation of GFP-tagged Hsp31p, the budding yeast environmental stress response chaperone, and glyoxalase III

2017 ◽  
Vol 23 (4) ◽  
pp. 595-607 ◽  
Author(s):  
Urszula Natkańska ◽  
Adrianna Skoneczna ◽  
Marek Skoneczny
Keyword(s):  
Oxidative Stress ◽  
Stress Response ◽  
Environmental Stress ◽  
Budding Yeast ◽  
Environmental Stress Response ◽  
Glyoxalase Iii

scholarly journals Identification of glutathione (GSH)-independent glyoxalase III from Schizosaccharomyces pombe

2014 ◽  
Vol 14 (1) ◽  
pp. 86 ◽  
Author(s):  
Qiaoqiao Zhao ◽  
Yang Su ◽  
Zhikang Wang ◽  
Caiping Chen ◽  
Tongsiyu Wu ◽  
...  
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Glyoxalase Iii

Overexpression of Glyoxalase III gene in transgenic sugarcane confers enhanced performance under salinity stress

2021 ◽  
Author(s):  
Manoj Vadakkenchery Mohanan ◽  
Anunanthini Pushpanathan ◽  
Sarath Padmanabhan ◽  
Thelakat Sasikumar ◽  
Ashwin Narayan Jayanarayanan ◽  
...  
Keyword(s):  
Salinity Stress ◽  
Transgenic Sugarcane ◽  
Glyoxalase Iii

Ectopic expression of DJ-1/PfpI domain containing Erianthus arundinaceus Glyoxalase III (EaGly III) enhances drought tolerance in sugarcane

2020 ◽  
Vol 39 (11) ◽  
pp. 1581-1594
Author(s):  
Manoj Vadakkenchery Mohanan ◽  
Anunanthini Pushpanathan ◽  
Sarath Padmanabhan Thelakat Sasikumar ◽  
Dharshini Selvarajan ◽  
Ashwin Narayan Jayanarayanan ◽  
...  
Keyword(s):  
Drought Tolerance ◽  
Ectopic Expression ◽  
Erianthus Arundinaceus ◽  
Glyoxalase Iii

scholarly journals Role of rpoS in the regulation of glyoxalase III in Escherichia coli.

2004 ◽  
Vol 51 (3) ◽  
pp. 857-860 ◽  
Author(s):  
Ludmil Benov ◽  
Fatima Sequeira ◽  
Anees F Beema
Keyword(s):  
Escherichia Coli ◽  
Stationary Phase ◽  
Enteric Bacteria ◽  
Glyoxalase I ◽  
Aldehyde Reductase ◽  
E Coli ◽  
Rpos Mutant ◽  
Phosphorylated Sugars ◽  
Glyoxalase Iii

Methylglyoxal is an endogenous electrophile produced in Escherichia coli by the enzyme methylglyoxal synthase to limit the accumulation of phosphorylated sugars. In enteric bacteria methylglyoxal is detoxified by the glutathione-dependent glyoxalase I/II system, by glyoxalase III, and by aldehyde reductase and alcohol dehydrogenase. Here we demonstrate that glyoxalase III is a stationary-phase enzyme. Its activity reached a maximum at the entry into the stationary phase and remained high for at least 20 h. An rpoS- mutant displayed normal glyoxalase I and II activities but was unable to induce glyoxalase III in stationary phase. It thus appears that glyoxalase III is regulated by rpoS and might be important for survival of non-growing E. coli cultures.

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