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BRENDA support

Literature summary for 4.4.1.5 extracted from

  • Birkenmeier, G.; Stegemann, C.; Hoffmann, R.; Guenther, R.; Huse, K.; Birkemeyer, C.
    Posttranslational modification of human glyoxalase 1 indicates redox-dependent regulation (2010), PLoS ONE, 5, e10399.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Homo sapiens 5829
-

Organism

Organism UniProt Comment Textmining
Homo sapiens Q04760
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glutathionylation glutathionylation strongly inhibits Glo1 activity in vitro Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
Homo sapiens
-

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
glutathione
-
Homo sapiens