The enzyme, described from the fungi Candida albicans and Schizosaccharomyces pombe, converts 2-oxopropanal to (R)-lactate in a single glutathione (GSH)-independent step. The other known route for this conversion is the two-step GSH-dependent pathway catalysed by EC 4.4.1.5 (lactoylglutathione lyase) and EC 3.1.2.6 (hydroxyacylglutathione hydrolase).
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
hsp31, glyoxalase iii, dj-1a, dj-1b, glutathione-independent glyoxalase, hsp3101, hsp3102, glutathione-independent glyoxalase iii, dj-1 glyoxalase, hsp31p glyoxalase iii, more
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SYSTEMATIC NAME
IUBMB Comments
(R)-lactate hydro-lyase
The enzyme, described from the fungi Candida albicans and Schizosaccharomyces pombe, converts 2-oxopropanal to (R)-lactate in a single glutathione (GSH)-independent step. The other known route for this conversion is the two-step GSH-dependent pathway catalysed by EC 4.4.1.5 (lactoylglutathione lyase) and EC 3.1.2.6 (hydroxyacylglutathione hydrolase).
the absence of the HSP31 gene sensitizes cells to oxidative, osmotic and thermal stresses, to potentially toxic products of glycolysis, such as methylglyoxal and acetic acid, and to the diauxic shift
overexpression of Hsp31 in tobacco imparts robust stress tolerance against diverse biotic stress inducers such as viruses, bacteria and fungi, in addition to tolerance against a range of abiotic stress inducers
fungal Hsp31 proteins are the major glyoxalases III GLO3 that may have some role in protecting cells from reactive carbonyl species toxicity in fungi. The GLO3 activity of Hsp31 proteins may have evolved independently from GLO3 activity of DJ-1 proteins. DJ-1 and Hsp31 proteins belong to different subfamilies of the DJ-1/Hsp31/PfpI superfamily, which encompasses a wide variety of functionally diverse proteins, detailed phylogenetic analysis of DJ-1 and Hsp31 proteins, distribution of Hsp31 proteins in fungi, overview
glyoxalase III is responsible for the detoxification of reactive carbonyl species, e.g. methylglyoxal and glyoxal, via the GSH-independent pathway, overview
two Schizosaccharomyces pombe Hsp31 proteins (Hsp3101 and Hsp3102) and one Saccharomyces cerevisiae Hsp31 protein (ScHsp31) display significantly higher in vitro GLO3 activity than Schizosaccharomyces pombe DJ-1 (SpDJ-1)
overexpression of Saccharomyces cerevisiae ScHSP31 confers methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1 deletion cells of Schizosaccharomyces pombe
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Nicotiana tabacum cv. Wisconsin. Overexpression of Hsp31 in tobacco imparts robust stress tolerance against diverse biotic stress inducers such as viruses, bacteria and fungi, in addition to tolerance against a range of abiotic stress inducers. During stress, Hsp31 is targeted to mitochondria and induces expression of key stress-related genes
gene ScHSP31, expression in Escherichia coli strain BL21(DE3), detailed phylogenetic analysis of GLOIII, DJ-1 and HSP31 proteins, overview. Overexpression of ScHSP31 can confer methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1-deletion of Schizosaccharomyces pombe
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
strong induction of this gene is caused by high concentrations of ethanol and other products of glycolysis. HSP31 gene expression is controlled by multiple transcription factors, including Yap1p, Cad1p, Msn2p, Msn4p, Haa1p and Hsf1p. These transcription factors mediate the HSP31 promoter responses to oxidative, osmotic and thermal stresses, to potentially toxic products of glycolysis, such as methylglyoxal and acetic acid, and to the diauxic shift
Natkanska, U.; Skoneczna, A.; Sienko, M.; Skoneczny, M.
The budding yeast orthologue of Parkinsons disease-associated DJ-1 is a multi-stress response protein protecting cells against toxic glycolytic products