| Post Translational Modifications | Glutathionylation at Cys-139 inhibits enzyme activity. Phosphorylated at Thr-107 in the presence of CaMK2. However, this is a consensus site for phosphorylation by CK2 so phosphorylation may be mediated by CK2 rather than CaMK2. Phosphorylation is induced by TNF and suppresses the TNF-induced transcriptional activity of NF-kappa-B. Exists in a nitric oxide (NO)-modified form. The exact nature of the modification is unknown, but it suppresses the TNF-induced transcriptional activity of NF-kappa-B. |
| Function | Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B. Required for normal osteoclastogenesis. |
| Protein Name | Lactoylglutathione LyaseAldoketomutaseGlyoxalase IGlx IKetone-Aldehyde MutaseMethylglyoxalaseS-D-Lactoylglutathione Methylglyoxal Lyase |
| Database Links | Reactome: R-HSA-70268 |
| Cellular Localisation | |
| Alternative Protein Names | Lactoylglutathione Lyase proteinAldoketomutase proteinGlyoxalase I proteinGlx I proteinKetone-Aldehyde Mutase proteinMethylglyoxalase proteinS-D-Lactoylglutathione Methylglyoxal Lyase proteinGLO1 protein |
Information sourced from Uniprot.org