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Literature summary for 4.4.1.5 extracted from

  • Staniszewska, M.M.; Nagaraj, R.H.
    Upregulation of glyoxalase I fails to normalize methylglyoxal levels: a possible mechanism for biochemical changes in diabetic mouse lenses (2006), Mol. Cell. Biochem., 288, 29-36.
    View publication on PubMed
Search for more literature for 4.4.1.5

Activating Compound

Activating Compound Comment Organism Structure
D-glucose 25 mM upregulates glyoxalase I activity and mRNA in LE cells when compared with either cells cultured with 5 mM glucose as control or with 20 mM L-glucose + 5 mM D-glucose Mus musculus

Application

Application Comment Organism
medicine upregulation of glyoxalase I in diabetes, this upregulation is inadequate to normalize methylglyoxal levels, which can lead to methylglyoxal retention and chemical modification of proteins Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Mus musculus 5829
-

Organism

Organism UniProt Comment Textmining
Mus musculus
-
 Balb/c mice, C57BL6/J female mice
-

Source Tissue

Source Tissue Comment Organism Textmining
lens glyoxalase I activity and mRNA levels are elevated in diabetic lenses Mus musculus
-
additional information LE cell, lens epithelial cells, activity of the enzyme in hyperglycemic conditions is nearly 20% higher than in control conditions Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione + methylglyoxal
-
 Mus musculus S-D-lactoylglutathione
-
 ?

Synonyms

Synonyms Comment Organism
glyoxalase I
-
 Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Mus musculus