MGP Database

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MGP001229

UniProt Annotations

Entry Information
Gene Nameglyoxalase I
Protein EntryLGUL_HUMAN
UniProt IDQ04760
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q04760-1; Sequence=Displayed; Name=2; IsoId=Q04760-2; Sequence=VSP_041632; Note=No experimental confirmation available.;
Biophysicochemical PropertiesKinetic parameters: KM=1.3 mM for methylglyoxal/glutathione (native form) {ECO:0000269|PubMed:20454679}; KM=0.7 mM for methylglyoxal/glutathione (reduced form) {ECO:0000269|PubMed:20454679}; Vmax=0.335 umol/min/mg enzyme with methylglyoxal/glutathione as substrate (native form) {ECO:0000269|PubMed:20454679}; Vmax=0.7 umol/min/mg enzyme with methylglyoxal/glutathione as substrate (reduced form) {ECO:0000269|PubMed:20454679}; Note=Reduction of GLO1 was carried out by incubation with 20 mM betamercaptoethanol prior to kinetic analysis.;
Catalytic Activity(R)-S-lactoylglutathione = glutathione + methylglyoxal. {ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9705294}.
CofactorName=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9705294}; Note=Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits. {ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9705294};
Enzyme RegulationRegulated by oxidation of Cys-139 in response to the redox state of the cell. Results in the alternative formation of cystine or glutathione-bound cysteine, the latter modification leading to reduced enzyme activity. {ECO:0000269|PubMed:20454679}.
FunctionCatalyzes 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. {ECO:0000269|PubMed:19199007, ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9705294}.
Mass SpectrometryMass=20629.7; Method=Electrospray; Range=2-184 (Q04760-1); Note=Variant Ala-111.; Evidence={ECO:0000269|PubMed:20454679};
Mass SpectrometryMass=20687.4; Method=Electrospray; Range=2-184 (Q04760-1); Note=Variant Glu-111.; Evidence={ECO:0000269|PubMed:20454679};
PathwaySecondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2.
PolymorphismExists in three separable isoforms which originate from two alleles in the genome. These correspond to two homodimers and one heterodimer composed of two subunits showing different electrophoretic properties.
PtmExists 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.
PtmGlutathionylation at Cys-139 inhibits enzyme activity. {ECO:0000269|PubMed:20454679}.
PtmPhosphorylated 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. {ECO:0000269|PubMed:17576200, ECO:0000269|PubMed:19199007}.
Sequence CautionSequence=BAD93038.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
SimilarityBelongs to the glyoxalase I family. {ECO:0000305}.
SubunitHomodimer. {ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294}.
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