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Literature summary for 4.4.1.5 extracted from

  • Hanssen, N.M.; Stehouwer, C.D.; Schalkwijk, C.G.
    Methylglyoxal and glyoxalase I in atherosclerosis (2014), Biochem. Soc. Trans., 42, 443-449.
    View publication on PubMed
Search for more literature for 4.4.1.5

Inhibitors

Inhibitors Comment Organism Structure
additional information posttranslational modification of Glo1 by oxidized glutathione (GSSG) and nitrosylation strongly inhibits Glo1 activity Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein the enzyme is susceptible to post-translational modifications, in particular phosphorylation in response to TNFalpha, a key mediator of inflammation Homo sapiens
side-chain modification posttranslational modification of Glo1 by oxidized glutathione (GSSG) and nitrosylation strongly inhibits Glo1 activity Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
blood vessel the enzyme is absent from the necrotic core of atherosclerotic plaques Homo sapiens
-
endothelial cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione + methylglyoxal
-
 Homo sapiens (R)-S-lactoylglutathione
-
 ?

Synonyms

Synonyms Comment Organism
Glo1
-
 Homo sapiens
glyoxalase I
-
 Homo sapiens

Expression

Organism Comment Expression
Homo sapiens the promoter of Glo1 harbours an nuclear factor kappaB-responsive element, indicating a link between inflammation and reduced Glo1 expression down

General Information

General Information Comment Organism
metabolism rate-limiting enzyme in the glyoxalase system Homo sapiens
physiological function methylglyoxal is a key player in vascular dysfunction, particularly due to its capacity to induce the formation of oxidative stress, cell death andendothelial dysfunction, glyoxylase I is the rate-limiting enzyme in the glyoxalase system for detoxifcation of methylglyoxal, accumulation of methylglyoxal and methylglyoxal-derived advanced glycation end-products may be a major contributing factor to atherosclerotic plaque rupture. Intracellular accumulation of methylglyoxal in endothelial cells causes dysfunction as indicated by expression of adhesion molecules such as vascular cell adhesion molecule 1 expression, which can be prevented by Glo1 overexpression Homo sapiens