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UniProt functional annotation for Q04760 | ||
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| UniProt code: Q04760. |
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| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
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| 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. {ECO:0000269|PubMed:19199007, ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9705294}. |
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| Catalytic activity: | |
Reaction=(R)-S-lactoylglutathione = glutathione + methylglyoxal; Xref=Rhea:RHEA:19069, ChEBI:CHEBI:17158, ChEBI:CHEBI:57474, ChEBI:CHEBI:57925; EC=4.4.1.5; Evidence={ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9705294}; |
| Cofactor: | |
Name=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}; |
| Activity regulation: | |
Regulated 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}. |
| Biophysicochemical properties: | |
Kinetic 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.; |
| Pathway: | |
Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2. |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294}. |
| Ptm: | |
Glutathionylation at Cys-139 inhibits enzyme activity. {ECO:0000269|PubMed:20454679}. |
| Ptm: | |
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. {ECO:0000269|PubMed:17576200, ECO:0000269|PubMed:19199007}. |
| Ptm: | |
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. |
| Mass spectrometry: | |
[Isoform 1]: Mass=20687.4; Method=Electrospray; Note=Variant Glu-111. The measured range is 2-184.; Evidence={ECO:0000269|PubMed:20454679}; |
| Mass spectrometry: | |
[Isoform 1]: Mass=20629.7; Method=Electrospray; Note=Variant Ala-111. The measured range is 2-184.; Evidence={ECO:0000269|PubMed:20454679}; |
| Polymorphism: | |
Exists 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. |
| Similarity: | |
Belongs to the glyoxalase I family. {ECO:0000305}. |
| Sequence caution: | |
Sequence=BAD93038.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; |
Annotations taken from UniProtKB at the EBI.